Research Topics
Genomes and Genes
| A WlodawerSummaryAffiliation: National Cancer Institute Country: USA Publications
| Collaborators
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Detail Information
Publications
A model of the ternary complex of interleukin-10 with its soluble receptorsSergei Pletnev
Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, MD 21702 1201, USA
BMC Struct Biol 5:10. 2005..This so far has prevented any attempts to obtain structural information about the ternary complex of IL-10 with its receptor chains...- A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidasesAlexander Wlodawer
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702, USA
BMC Struct Biol 3:8. 2003..Similar enzymes have been found in the genomic sequences of several species, but neither systematic analyses of their distribution nor modeling of their structures have been previously attempted... - Structural and biochemical studies of retroviral proteasesA Wlodawer
Macromolecular Crystallography Laboratory, Program in Structural Biology, NCI Frederick Cancer Research and Development Center, Frederick, MD 21702, USA
Biochim Biophys Acta 1477:16-34. 2000..In this review, structural and biochemical data for retroviral proteases are compared in order to analyze the similarities and differences between the enzymes from different sources and to enhance our understanding of their properties... - Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymesA Wlodawer
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Maryland 21702, USA
Nat Struct Biol 8:442-6. 2001..Thus, the structure of PSCP defines a novel family of serine-carboxyl proteinases (defined as MEROPS S53) with a unique catalytic triad consisting of Glu 80, Asp 84 and Ser 287... - Inhibitors of HIV-1 protease: a major success of structure-assisted drug designA Wlodawer
Macromolecular Structure Laboratory, ABL Basic Research Program, National Cancer Institute Frederick Cancer Research and Development Center, Maryland 21702, USA
Annu Rev Biophys Biomol Struct 27:249-84. 1998..The structural basis of drug resistance and the ways of overcoming this phenomenon are mentioned... - Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidasesAlexander Wlodawer
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702, USA
Acta Biochim Pol 50:81-102. 2003..This review compares the structural and enzymatic properties of this newly defined MEROPS family of peptidases, S53, and introduces their new nomenclature... - Inhibitor complexes of the Pseudomonas serine-carboxyl proteinaseA Wlodawer
Protein Structure Section, Macromolecular Crystallography Laboratory, and Intramural Research Support Program, SAIC Frederick, National Cancer Institute at Frederick, Frederick, Maryland 21702, USA
Biochemistry 40:15602-11. 2001..The presence of Ca(2+) cation is necessary for the activity of the enzyme... - Rational approach to AIDS drug design through structural biologyAlexander Wlodawer
Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland 21702, USA
Annu Rev Med 53:595-614. 2002..This review presents the methods used to develop such drugs and discusses the remaining problems, such as the rapid emergence of drug resistance... - Structure-based design of AIDS drugs and the development of resistanceAlexander Wlodawer
Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD, USA
Vox Sang 83:23-6. 2002.... - Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrateAlexander Wlodawer
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702, USA
Biochem Biophys Res Commun 314:638-45. 2004..The kinetic parameters for the substrate, measured by the increase in fluorescence upon relief of quenching, were: k(cat)=73+/-5 s(-1), K(m)=0.12+/-0.011 microM, and k(cat)/K(m)=608+/-85 s(-1)microM(-1)... - Crystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activityAlexander Wlodawer
Protein Structure Section, Macromolecular Crystallography Laboratory, NCI Frederick, National Institutes of Health, Frederick, MD 21702, USA
J Biol Chem 279:21500-10. 2004..01% activity of the wild-type enzyme, and its structure revealed that Ser(278), His(78), and Asp(82) do not interact with each other; thus, the canonical catalytic triad is disrupted... - Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structuresAlexander Wlodawer
Macromolecular Crystallography Laboratory, NCI, Frederick, MD 21702, USA
FEBS J 275:1-21. 2008.... - Novel fold and capsid-binding properties of the lambda-phage display platform protein gpDF Yang
Macromolecular Crystallography Laboratory, Program in Structural Biology, National Cancer Institute, Frederick Cancer Research and Development Center, Frederick, Maryland 21702, USA
Nat Struct Biol 7:230-7. 2000..Despite this orientation of the gpD trimer, fusion proteins connected by linker peptides to either terminus bind to the capsid, allowing protein and peptide display... - Crystal structure and amino acid sequence of Wolinella succinogenes L-asparaginaseJ Lubkowski
Macromolecular Structure Laboratory, NCI Frederick Cancer Research and Development Center, ABL Basic Research Programm, Frederick, Maryland, USA
Eur J Biochem 241:201-7. 1996..The rigid part of the active site, which includes the asparaginase triad Thr93-Lys 166-Asp94, is structurally very highly conserved with equivalent regions found in other type-II bacterial L-asparaginases... - Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginaseK Aghaiypour
Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland 21702, USA
Biochemistry 40:5655-64. 2001.... - Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapyA L Swain
Macromolecular Structure Laboratory, National Cancer Institute Frederick Cancer Research and Development Center, MD 21702 1201
Proc Natl Acad Sci U S A 90:1474-8. 1993.... - Crystal structure of human interleukin-10 at 1.6 A resolution and a model of a complex with its soluble receptorA Zdanov
Macromolecular Structure Laboratory, NCI Frederick Cancer Research and Development Center, ABL Basic Research Program, Frederick, Maryland 21702, USA
Protein Sci 5:1955-62. 1996..The contact region between the cytokine and each receptor shows excellent complementarity of polar and hydrophobic interactions, suggesting that the model is generally correct and should be useful in guiding mutagenesis experiments... - A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutantG J Palm
Macromolecular Structure Laboratory, NCI Frederick Cancer Research and Development Center, Frederick, MD 21702 1201, USA
FEBS Lett 390:211-6. 1996..Kinetic analysis confirms the deacylation deficiency, which is also explained on a structural basis. The previously identified oxyanion hole is described in more detail... - Do bacterial L-asparaginases utilize a catalytic triad Thr-Tyr-Glu?K Aghaiypour
Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702, USA
Biochim Biophys Acta 1550:117-28. 2001.... - Purification of receptor complexes of interleukin-10 stoichiometry and the importance of deglycosylation in their crystallizationD M Hoover
Macromolecular Structure Laboratory, NCI Frederick Cancer Research and Development Center, ABL Basic Research Program, Frederick, MD, USA
Eur J Biochem 262:134-41. 1999..The availability of the structure of the ligand-receptor complexes should facilitate our understanding of the basis of the interaction between IL-10 and the IL-10 receptor... - Crystal structure of a cyclic form of bovine pancreatic trypsin inhibitorI Botos
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, MD 21702, USA
FEBS Lett 509:90-4. 2001.... - Crystal structure of RNA 3'-terminal phosphate cyclase, a ubiquitous enzyme with unusual topologyG J Palm
Program in Structural Biology, Macromolecular Crystallography Laboratory, National Cancer Institute FCRDC, Frederick, MD 21702, USA
Structure 8:13-23. 2000..These enzymes might be responsible for production of the cyclic phosphate RNA ends that are known to be required by many RNA ligases in both prokaryotes and eukaryotes... - Crystal structures of catalytic core domains of retroviral integrases and role of divalent cations in enzymatic activityA Wlodawer
Macromolecular Structure Laboratory, NCI Frederick Cancer Research and Development Center, Maryland 21702, USA
Adv Virus Res 52:335-50. 1999..Here the role of divalent cations in the enzymatic activity of IN and the search for inhibitors of this enzyme are discussed... - Structural characterization of Pseudomonas 7A glutaminase-asparaginaseJ Lubkowski
Macromolecular Structure Laboratory, NCI Frederick Cancer Research and Development Center, Maryland 21702 1201
Biochemistry 33:10257-65. 1994.... - Crystal structure of the dimeric C-terminal domain of TonB reveals a novel foldC Chang
Macromolecular Crystallography Laboratory, NCI, National Institutes of Health, Frederick, Maryland 21702, USA
J Biol Chem 276:27535-40. 2001..The two monomers are intertwined with each other, and all six beta-strands of the dimer make a large antiparallel beta-sheet. We propose a plausible model of binding of TonB to FhuA and FepA, two TonB-dependent outer-membrane receptors... - Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gammaA Zdanov
Macromolecular Structure Laboratory, NCI Frederick Cancer Research and Development Center, Maryland 21702, USA
Structure 3:591-601. 1995..An atomic model is necessary to interpret biological activity of IL-10 and to design mutants with agonistic or antagonistic properties... - A left-handed crossover involved in amidohydrolase catalysis. Crystal structure of Erwinia chrysanthemi L-asparaginase with bound L-aspartateM Miller
Macromolecular Structure Laboratory, NCI FCRDC, Frederick, MD 21702
FEBS Lett 328:275-9. 1993..The orientation of the bound aspartate indicates for the first time a threonine residue as a catalytic nucleophile... - Cyanovirin-N: a sugar-binding antiviral protein with a new twistI Botos
National Cancer Institute, MCL, Bldg. 536, Rm. 5, Frederick, Maryland 21702-1201, USA
Cell Mol Life Sci 60:277-87. 2003..Structures of several complexes of CV-N with oligosaccharides help in explaining the unique mode of high-affinity binding of these molecules to both forms of CV-N... - Structure and mechanism of activity of the cyclic phosphodiesterase of Appr>p, a product of the tRNA splicing reactionA Hofmann
Protein Structure Section, Macromolecular Crystallography Laboratory, Program in Structural Biology, NCI Frederick, Frederick, MD 21702, USA
EMBO J 19:6207-17. 2000.... - Practical experience with the use of halides for phasing macromolecular structures: a powerful tool for structural genomicsZ Dauter
Synchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, Program in Structural Biology, National Cancer Institute and NSLS, Brookhaven National Laboratory, Building 725A X9, Upton, NY 11973, USA
Acta Crystallogr D Biol Crystallogr 57:239-49. 2001..In conclusion, the use of halides with single-wavelength diffraction data fulfills the requirements of being a first-choice method of high-throughput structure solution for the emerging field of structural genomics... - Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolAJ Lubkowski
Macromolecular Structure Laboratory, NCI Frederick Cancer Research and Development Center, MD 21702, USA
Structure 7:711-22. 1999.... - [Tobacco etch virus proteinase: crystal structure of the active enzyme and its inactive mutant]A S Zhdanov
Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, MD 21702 1201, United States
Bioorg Khim 29:457-60. 2003..This indicates that the autolysis of the peptide bond Met218-Ser219 exerts a strong effect on the fine-tuning of the substrate in the enzyme active site, which results in considerable decrease in the enzymatic activity... - The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactionsJ Lubkowski
Macromolecular Structure Laboratory, NCI Frederick Cancer Research and Development Center, ABL Basic Research Program, Maryland 21702, USA
Nat Struct Biol 4:64-9. 1997..These data can be used to explain the structural basis for the assignment of residues responsible for biological activity... - Crystal structure of Escherichia coli HdeAF Yang
Macromolecular Structure Laboratory, ABL-Basic Research Program, DTP, NCI-FCRDC, Frederick, Maryland 21702-1201, USA
Nat Struct Biol 5:763-4. 1998 - Crystal structure of rabbit muscle creatine kinaseJ K Rao
Macromolecular Structure Laboratory, NCI Frederick Cancer Research and Development Center, ABL Basic Research Program, Frederick, MD 21702, USA
FEBS Lett 439:133-7. 1998..The putative binding site of creatine, which is occupied by a sulfate group in this analysis, has been tentatively identified. The dimeric interface of the enzyme is held together by a small number of hydrogen bonds... - Crystal structure of a Y35G mutant of bovine pancreatic trypsin inhibitorD Housset
Macromolecular Structure Laboratory, NCI Frederick Cancer Research and Development Center, MD 21702
J Mol Biol 220:757-70. 1991..Seventy water molecules were included in the model but only seven of them are shared with the native structure. Thermal parameters are showing a good correlation with those for the wild-type of BPTI... - PCSB--a program collection for structural biology and biophysical chemistryA Hofmann
Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, National Institutes of Health, Frederick, MD 21702, USA
Bioinformatics 18:209-10. 2002..All applications are portable to different platforms and require only the Java Runtime Environment to be installed on the system. available as PDF file... - Catalytic residues and substrate specificity of recombinant human tripeptidyl peptidase I (CLN2)Hiroshi Oyama
Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology, Matsugasaki, Sakyo ku
J Biochem 138:127-34. 2005..TPP-I might have evolved from an ancestral gene in order to cleave, in cooperation with cathepsins, useless proteins in the lysosomal compartment... - 1,2,3-triazole as a peptide surrogate in the rapid synthesis of HIV-1 protease inhibitorsAshraf Brik
Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
Chembiochem 6:1167-9. 2005 - Autophosphorylation of Archaeoglobus fulgidus Rio2 and crystal structures of its nucleotide-metal ion complexesNicole LaRonde-LeBlanc
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, NCI Frederick, MD 21702 1201, USA
FEBS J 272:2800-10. 2005..These results give us further information about the nature of the active site of Rio2 kinase and suggest a mechanism of regulation of its enzymatic activity... - Crystal structure of the N-terminal domain of E. coli Lon proteaseMi Li
Macromolecular Crystallography Laboratory, National Cancer Institute, Building 536, Room 5, Frederick, MD 21702 1201, USA
Protein Sci 14:2895-900. 2005..We postulate that, as is the case in Lon proteases, this structural domain represents a general protein and polypeptide interaction domain... - Crystal structure of human T cell leukemia virus protease, a novel target for anticancer drug designMi Li
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA
Proc Natl Acad Sci U S A 102:18332-7. 2005..The structure presented here can be used as a starting point for the development of such anticancer therapies... - Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteasesIstvan Botos
Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702 1201, USA
J Mol Biol 351:144-57. 2005.... - Structure and activity of the atypical serine kinase Rio1Nicole LaRonde-LeBlanc
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, NCI Frederick, MD 21702 1201, USA
FEBS J 272:3698-713. 2005..In addition, we show that a mutant enzyme that cannot be autophosphorylated can still phosphorylate an inactive form of Rio1, as well as a number of typical kinase substrates... - A general acid-base mechanism for the stabilization of a tetrahedral adduct in a serine-carboxyl peptidase: a computational studyHaobo Guo
Department of Biochemistry and Cellular and Molecular Biology and Center of Excellence for Structural Biology, University of Tennessee, Knoxville, Tennessee 37996, USA
J Am Chem Soc 127:15662-3. 2005.... - The importance of dynamics in substrate-assisted catalysis and specificityQin Xu
Department of Biochemistry and Cellular and Molecular Biology, and Center of Excellence for Structural Biology, University of Tennessee, Knoxville, Tennessee 37996, USA
J Am Chem Soc 128:5994-5. 2006..The QM/MM MD and free energy simulations show that the dynamics involving a His residue at the P1 site of the substrate may play an important role in substrate-assisted catalysis and specificity for a serine-carboxyl peptidase... - Processing, catalytic activity and crystal structures of kumamolisin-As with an engineered active siteAyumi Okubo
Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Sendai, Japan
FEBS J 273:2563-76. 2006..These results corroborate the mechanistic importance of the glutamate-mediated catalytic triad and oxyanion-stabilizing aspartic acid residue for low-pH peptidase activity of the enzyme... - Crystal structure of a dimerized cockroach allergen Bla g 2 complexed with a monoclonal antibodyMi Li
Macromolecular Crystallography Laboratory, NCI Frederick, National Institutes of Health, Frederick, Maryland 21702, USA
J Biol Chem 283:22806-14. 2008..We have now identified key residues involved in IgE antibody binding; this information will be useful for the design of vaccines for immunotherapy... - Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragmentsEdward E Melnikov
Shemyakin Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
Acta Biochim Pol 55:281-96. 2008.... - Determination of protein structures--a series of fortunate eventsMaksymilian Chruszcz
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA
Biophys J 95:1-9. 2008..This review examines the difficulties presented by each step on the path from a gene to the final publication, together with certain lucky (or unlucky) circumstances that can affect the velocity along that path... - A new look at cytokine signalingAlexander Zdanov
Macromolecular Crystallography Laboratory, CCR, National Cancer Institute at Frederick, Frederick, MD 21702, USA
Cell 132:179-81. 2008..2008) present crystal structures of three signaling complexes of the cytokines interleukin-4 and interleukin-13 with their receptors, showing how events taking place outside the cell may affect the specificity of signal transduction... - Refined crystal structures of red and green fluorescent proteins from the button polyp ZoanthusNadezhda Pletneva
Shemyakin Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Science, Moscow, Russia
Acta Crystallogr D Biol Crystallogr 63:1082-93. 2007..These residues present initial useful targets for rational mutagenesis aimed at designing monomeric forms of the fluorescent proteins, which are more suitable for practical applications... - Structural characterization of B and non-B subtypes of HIV-protease: insights into the natural susceptibility to drug resistance developmentMario Sanches
Grupo de Cristalografia, Instituto de Fisica de Sao Carlos, Universidade de Sao Paulo, Av Trabalhador Saocarlense, 400, CEP 13560 970, Sao Carlos, SP, Brazil
J Mol Biol 369:1029-40. 2007..Our results further indicate that two naturally occurring polymorphic substitutions in subtype F and other non-B HIV proteases, M36I and L89M, may lead to early development of drug resistance in patients infected with non-B HIV subtypes... - Crystallographic, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsinNatasza E Ziółkowska
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, NCI Frederick, Frederick, Maryland 21702 1201, USA
Proteins 67:661-70. 2007..The ability to mediate tight multivalent and multisite interactions with high-mannose oligosaccharides helps to explain the potent antiviral activity of griffithsin... - Deposition of structural data reduxAlexander Wlodawer
Acta Crystallogr D Biol Crystallogr 63:421-3. 2007 - The QM/MM molecular dynamics and free energy simulations of the acylation reaction catalyzed by the serine-carboxyl peptidase kumamolisin-AsQin Xu
Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996, USA
Biochemistry 46:3784-92. 2007.... - Structural basis for inhibition of translation by the tumor suppressor Pdcd4Nicole LaRonde-LeBlanc
Macromolecular Crystallography Laboratory, CCR, National Cancer Institute, Frederick, MD 21702, USA
Mol Cell Biol 27:147-56. 2007..Finally, our structural analysis reveals MA3 domains to be a novel subfamily of VHS domains... - Catalytic role of proton transfers in the formation of a tetrahedral adduct in a serine carboxyl peptidaseHaobo Guo
Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996, USA
Biochemistry 45:9129-37. 2006..The effects of proton shuffling from Asp82 to Glu78 and from Glu32 to Asp82 are examined, and the results indicate that such proton shuffling may not play an important role in the stabilization of the tetrahedral intermediate analogue... - Statistical coupling analysis of aspartic proteinases based on crystal structures of the Trichoderma reesei enzyme and its complex with pepstatin AAlessandro S Nascimento
Grupo de Cristalografia, Departamento de Fisica e Informatica, Instituto de Fisica de Sao Carlos, Universidade de Sao Paulo, Av Trabalhador Saocarlense, 400, CEP 13560 970, Sao Carlos, Sao Paulo, Brazil
J Mol Biol 382:763-78. 2008.... - Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibitionAlla Gustchina
Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA
J Mol Biol 348:433-44. 2005..Five disulfide bridges and a Zn-binding site confer stability to the protein, which may contribute to sensitization at lower levels of exposure than other allergens... - Crystal structures of the semireduced and inhibitor-bound forms of cyclic nucleotide phosphodiesterase from Arabidopsis thalianaAndreas Hofmann
Macromolecular Crystallography Laboratory, NCI, National Institutes of Health, Frederick, Maryland 21702, USA
J Biol Chem 277:1419-25. 2002..The ligand is bound within the active site, and the mode of binding is in agreement with the previously proposed enzymatic mechanism. Selected biophysical properties of the oxidized and the semireduced CPDase are also discussed... - Biophysical characterization of cyclic nucleotide phosphodiesterasesAndreas Hofmann
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, National Institutes of Health, Frederick, Maryland 21702, USA
Biochem Biophys Res Commun 291:875-83. 2002..Within the comparison of the three proteins in this study, the PDase Homolog/RNA ligase (E. coli) shares more similarities with the plant than with the yeast protein... - Crystal structure of interleukin-19 defines a new subfamily of helical cytokinesChangsoo Chang
Protein Structure Section, Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute Frederick, National Institutes of Health, Maryland 21702 1201, USA
J Biol Chem 278:3308-13. 2003..On the basis of the observed structure, we propose that IL-19, IL-20, and other putative members of the proposed IL-10 family together form a distinct subfamily of helical cytokines... - Structural basis for the substrate specificity of tobacco etch virus proteaseJason Phan
Macromolecular Crystallography Laboratory, Center for Cancer Research, NCI-Frederick, National Institutes of Health, Frederick, Maryland 21702-1201, USA
J Biol Chem 277:50564-72. 2002..Analysis of the protein-ligand interactions helps to delineate the structural determinants of substrate specificity and provides guidance for reengineering the enzyme to further improve its utility for biotechnological applications... - Crystallization of cyclase-associated protein from Dictyostelium discoideumAndreas Hofmann
Macromolecular Crystallography Laboratory, NCI at Frederick, Frederick, MD 21702, USA
Acta Crystallogr D Biol Crystallogr 58:1858-61. 2002..A complete native data set extending to 2.2 A resolution was collected from a single crystal using an in-house X-ray system. The asymmetric unit contains one molecule of CAP... - Structure of cyclized green fluorescent proteinAndreas Hofmann
Macromolecular Crystallography Laboratory, NCI at Frederick, Frederick, MD 21702, USA
Acta Crystallogr D Biol Crystallogr 58:1400-6. 2002..This adds further support to the fact that the cylinder surface of GFP is rather versatile and can employ various polar and non-polar patches in protein-protein interactions... - Plant annexins form calcium-independent oligomers in solutionAndreas Hofmann
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, Maryland 21702, USA
Protein Sci 11:2033-40. 2002..Anx(Gh2) showed a different elution profile than the other plant annexins; while having only a very small trimer content, this annexin seems to exist in a monomer-dimer equilibrium in solution... - An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiaeAlla Gustchina
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702-1201, USA
Biochem Biophys Res Commun 295:1020-6. 2002.... - Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharidesIstvan Botos
Macromolecular Crystallography Laboratory, National Cancer Institute/National Institutes of Health, MCL Building 536, Frederick, MD 21702-1201, USA
J Biol Chem 277:34336-42. 2002..These structures show unequivocally the binding geometry of high mannose sugars to CV-N, permitting a better understanding of carbohydrate binding to this potential new lead for the design of drugs against AIDS... - The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structuresLaura G Barrientos
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Structure 10:673-86. 2002..By contrast, mutation of the neighboring serine to proline results in an exclusively dimeric protein, caused by a drastic destabilization of the monomer... - Retroviral proteasesBen M Dunn
Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32610, USA
Genome Biol 3:REVIEWS3006. 2002..The need to develop new drugs against HIV will continue to be, to a large extent, the driving force behind further characterization of retroviral proteases... - Crystallographic and functional studies of a modified form of eosinophil-derived neurotoxin (EDN) with novel biological activitiesChangsoo Chang
Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA
J Mol Biol 317:119-30. 2002.... - Atomic resolution structure of Erwinia chrysanthemi L-asparaginaseJacek Lubkowski
Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702, USA
Acta Crystallogr D Biol Crystallogr 59:84-92. 2003..This atomic resolution structure is a step in that direction... - Domain-swapped structure of a mutant of cyanovirin-NIstvan Botos
Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702-1201, USA
Biochem Biophys Res Commun 294:184-90. 2002..The current structure contributes to the understanding of domain swapping in cyanovirins, permitting rational design of domain-swapped CV-N mutants... - Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domainsTatyana V Rotanova
Shemyakin Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
Eur J Biochem 271:4865-71. 2004..These differences strictly associate with the specific characteristics of their AAA+ modules, as well as with the presence or absence of an N-terminal domain... - Proteins that bind high-mannose sugars of the HIV envelopeIstvan Botos
Macromolecular Crystallography Laboratory, National Cancer Institute, NCI Frederick, Building 536, Room 5, Frederick, MD 21702 1201, USA
Prog Biophys Mol Biol 88:233-82. 2005..This review summarizes, principally from a structural point of view, the current state of knowledge about these high-mannose binding proteins and their mode of sugar binding... - Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP)Adlina Mohd Yusof
Institute of Structural and Molecular Biology, School of Biological Sciences, The University of Edinburgh, Scotland, United Kingdom
Proteins 58:255-62. 2005..Comparison with previously published structures of N-CAP reveals variable modes of dimerization of this domain, but the presence of a common interface for the side-to-side dimer... - Kinetic stability and crystal structure of the viral capsid protein SHPPatrik Forrer
Biochemisches Institut, Universitat Zurich, Winterthurerstrasse 190, CH 8057 Zurich, Switzerland
J Mol Biol 344:179-93. 2004..Kinetic stability may be especially needed in phage capsids to allow survival in harsh environments... - Crystal structure of A. fulgidus Rio2 defines a new family of serine protein kinasesNicole LaRonde-LeBlanc
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, NCI Frederick, MD 21702, USA
Structure 12:1585-94. 2004..These discoveries have implications in determining the target and function of RIO proteins and define a distinct new family of protein kinases... - Crystal structure of a truncated version of the phage lambda protein gpDChangsoo Chang
Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland 21702, USA
Proteins 57:866-8. 2004 - Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolutionIstvan Botos
Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, MCL Bldg 536, Rm 5, Frederick, MD 21702 1201, USA
J Struct Biol 146:113-22. 2004..Detailed comparison with the structures of 11 similar domains established the putative location of the nucleotide-binding site in this first fragment of Lon for which a crystal structure has become available... - The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active siteIstvan Botos
Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland 21702 1201, USA
J Biol Chem 279:8140-8. 2004.... - Characterization of the recombinant extracellular domains of human interleukin-20 receptors and their complexes with interleukin-19 and interleukin-20Sergei Pletnev
Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Maryland 21702 1201, USA
Biochemistry 42:12617-24. 2003.... - Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthaseSabine Breinig
Fox Chase Cancer Center, 333 Cottman Avenue, Philadelphia, Pennsylvania 19111-2497, USA
Nat Struct Biol 10:757-63. 2003.... - The crystal structure of annexin Gh1 from Gossypium hirsutum reveals an unusual S3 clusterAndreas Hofmann
Institute of Cell and Molecular Biology, The University of Edinburgh, Edinburgh, Scotland
Eur J Biochem 270:2557-64. 2003..We therefore hypothesize that the cysteine motif found in the present structure, or possibly even the entire sulfur cluster, forms the molecular basis for annexin function in oxidative stress response... - Species-specific inhibition of porphobilinogen synthase by 4-oxosebacic acidEileen K Jaffe
Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111, USA
J Biol Chem 277:19792-9. 2002..A comparison of these with other PBGS structures identifies highly conserved active site water molecules, which are isolated from bulk solvent and implicated as proton acceptors in the PBGS-catalyzed reaction... - Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domainsTatyana V Rotanova
Shemyakin Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow
Protein Sci 15:1815-28. 2006..These first glimpses of the structure of Lon are heralding an exciting new era of research on this ancient family of proteases... - Comparison of the substrate specificity of two potyvirus proteasesJozsef Tozser
Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, University of Debrecen, Debrecen, Hungary
FEBS J 272:514-23. 2005..Additional residues in the substrate-binding subsites of TEV protease were also mutated in an effort to alter the specificity of the enzyme...