Research Topics
Genomes and Genes | L TongSummaryAffiliation: Columbia University Country: USA Publications
| Collaborators
|
Detail Information
Publications
How to take advantage of non-crystallographic symmetry in molecular replacement: 'locked' rotation and translation functionsL Tong
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Acta Crystallogr D Biol Crystallogr 57:1383-9. 2001..Moreover, the locked functions reduce the noise level in the calculation, owing to the averaging over the NCS elements, and increase the signals as all monomers of the assembly are taken into account at the same time...- Pyrazole urea-based inhibitors of p38 MAP kinase: from lead compound to clinical candidateJohn Regan
Department of Medicinal Chemistry, Research and Development Center, Boehringer Ingelheim Pharmaceuticals, 900 Ridgebury Road, Ridgefield, CT 06877, USA
J Med Chem 45:2994-3008. 2002..This modification affords significant improvements in binding, cellular, and in vivo potencies resulting in the selection of 45 (BIRB 796) as a clinical candidate for the treatment of inflammatory diseases... - Crystal structures of substrate complexes of malic enzyme and insights into the catalytic mechanismXiao Tao
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Structure 11:1141-50. 2003..Tyr112-Lys183 functions as the general acid-base pair to catalyze the tautomerization of the enolpyruvate product from decarboxylation to pyruvate... 
Structure and function of the phenazine biosynthetic protein PhzF from Pseudomonas fluorescensWulf Blankenfeldt
Max Planck Institute of Molecular Physiology, Otto Hahn Strasse 11, 44227 Dortmund, Germany
Proc Natl Acad Sci U S A 101:16431-6. 2004..Our proposed mechanism is supported by mass and NMR spectroscopy. The results are discussed in the context of related structures and protein sequences of unknown biochemical function...- A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural productYang Shen
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Mol Cell 16:881-91. 2004..Observations from native gel electrophoresis confirm this structural insight. The structural information provides a foundation for structure-based design of new inhibitors against these enzymes... - Acetyl-coenzyme A carboxylases: versatile targets for drug discoveryLiang Tong
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
J Cell Biochem 99:1476-88. 2006..This review summarizes these new progresses and also offers some prospects in terms of the future directions for the studies on these important enzymes... - Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discoveryL Tong
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Cell Mol Life Sci 62:1784-803. 2005..The current intense research on these enzymes could lead to the development of novel therapies against metabolic syndrome and other diseases... - Carboxymethyl-phenylalanine as a replacement for phosphotyrosine in SH2 domain bindingL Tong
Boehringer Ingelheim Pharmaceuticals, Inc, Ridgefield, Connecticut 06877, USA
J Biol Chem 273:20238-42. 1998.... - Conserved mode of peptidomimetic inhibition and substrate recognition of human cytomegalovirus proteaseL Tong
Boehringer Ingelheim Pharmaceuticals, Inc, Ridgefield, Connecticut 06877, USA
Nat Struct Biol 5:819-26. 1998..HCMV protease therefore represents example of convergent evolution. In addition, large conformational differences relative to the structure of the free enzyme are observed, which may be important for inhibitor binding... - Crystallization and preliminary crystallographic analysis of recombinant human P38 MAP kinaseS Pav
Department of Inflammatory Diseases, Boehringer Ingelheim Pharmaceuticals, Inc Ridgefield, Connecticut 06877, USA
Protein Sci 6:242-5. 1997..The cell parameters for crystal form 1 are a = 65.2 A, b = 74.6 A and c = 78.1 A. Those for crystal form 2 are a = 58.3 A, b = 68.3 A and c = 87.9 A. Diffraction data to 2.0 A resolution have been collected on both forms... - Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitorsP D Jeffrey
Cellular Biochemistry and Biophysics Program, Memorial Sloan Kettering Cancer Center, New York, New York 10021, USA
Genes Dev 14:3115-25. 2000..These observations support the model that INK4 binding weakens the cyclin's affinity for the CDK. This structure also provides insights into the specificity of the D-type cyclins for Cdk4/6... - Investigating the role of histidine 157 in the catalytic activity of human cytomegalovirus proteaseR Khayat
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Biochemistry 40:6344-51. 2001..Finally, structural comparisons revealed the presence of two conserved structural water molecules at the bottom of the S(1) pocket, suggesting a possible new direction for the design of HCMV protease inhibitors... - A new serine-protease fold revealed by the crystal structure of human cytomegalovirus proteaseL Tong
Boehringer Ingelheim Pharmaceuticals Inc, Ridgefield, Connecticut 06877, USA
Nature 383:272-5. 1996..A dimer of the protease with an extensive interface is found in the crystal structure. This structure information will help in the design and optimization of inhibitors against herpesvirus proteases... - Potent and competitive inhibition of malic enzymes by lanthanide ionsZ Yang
Department of Biological Sciences, Columbia University, New York, New York, 10027, USA
Biochem Biophys Res Commun 274:440-4. 2000.... - Structure of a closed form of human malic enzyme and implications for catalytic mechanismZ Yang
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Nat Struct Biol 7:251-7. 2000..Changes in tetramer organization of the enzyme are also observed in these complexes, which might be relevant for its cooperative behavior and allosteric control... - Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus proteaseR Batra
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Nat Struct Biol 8:810-7. 2001..Our studies suggest that appropriate dimer formation may be required to indirectly stabilize the protease oxyanion hole, revealing a novel mechanism for dimerization to regulate enzyme activity... - Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4aA A Russo
Cellular Biochemistry and Biophysics Program, Memorial Sloan Kettering Cancer Center, New York, New York 10021, USA
Nature 395:237-43. 1998..Tumour-derived mutations in INK4a and Cdk4 map to interface contacts, solidifying the role of CDK binding and inhibition in the tumour suppressor activity of p16INK4a... - Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamicsS Rozovsky
Department of Chemistry, Columbia University, New York, NY 10027, USA
J Mol Biol 310:271-80. 2001..The rate of ligand release is less than 1000 s(-1) at 0 degrees C and more than 1000 s(-1) at 30 degrees C. Therefore, loop motion and product release are probably concerted and likely to represent a rate limiting step for chemistry... - Structural basis for self-association and receptor recognition of human TRAF2Y C Park
Department of Biochemistry, The Weill Medical College and Graduate School of Medical Sciences of Cornell University, New York, New York 10021, USA
Nature 398:533-8. 1999..The trimeric structure of the TRAF domain provides an avidity-based explanation for the dependence of TRAF recruitment on the oligomerization of the receptors by their trimeric extracellular ligands... - Structural basis for signal transduction by the Toll/interleukin-1 receptor domainsY Xu
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Nature 408:111-5. 2000.... - Crystal structure of human mitochondrial NAD(P)+-dependent malic enzyme: a new class of oxidative decarboxylasesY Xu
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Structure 7:R877-89. 1999..Moreover, this isoform is unique among malic enzymes in that it is a cooperative enzyme, and its activity is controlled allosterically... - 2',6'-Dimethylphenoxyacetyl: a new achiral high affinity P(3)-P(2) ligand for peptidomimetic-based HIV protease inhibitorsP L Beaulieu
Boehringer Ingelheim Pharmaceuticals Inc, 175 Briar Ridge Road, Ridgefield, Connecticut 06877, USA
J Med Chem 43:1094-108. 2000.... - Binding site elucidation of hydantoin-based antagonists of LFA-1 using multidisciplinary technologies: evidence for the allosteric inhibition of a protein--protein interactionK Last-Barney
Research and Development Center, Boehringer Ingelheim Pharmaceuticals, 900 Ridgebury Road, P.O. Box 368, Ridgefield, Connecticut 06877, USA
J Am Chem Soc 123:5643-50. 2001..The atomic details of the protein/antagonist interaction were accurately predicted by this model, as subsequently confirmed by the X-ray crystal structure of the complex... - Viral proteasesLiang Tong
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Chem Rev 102:4609-26. 2002 - COMO: a program for combined molecular replacementG Jogl
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Acta Crystallogr D Biol Crystallogr 57:1127-34. 2001..A case is presented where the program automatically determined the orientation and position of five copies of a search model in a high-symmetry space group... - A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocketL Tong
Boehringer Ingelheim Pharmaceuticals, Inc, Ridgefield, Connecticut 06877, USA
Nat Struct Biol 4:311-6. 1997..Other protein kinase inhibitors may achieve their specificity through a similar mechanism. The structure also reveals a possible second binding site for this inhibitor, with currently unknown function... - Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofopHailong Zhang
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Proc Natl Acad Sci U S A 101:5910-5. 2004..Two residues that affect herbicide sensitivity are located in this binding site, and mutation of these residues disrupts the structure of the domain. Other residues in the binding site are strictly conserved among the CT domains... - Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylaseHailong Zhang
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Science 299:2064-7. 2003..Mutagenesis and kinetic studies reveal the functional roles of conserved residues here. The herbicides target the active site of CT, providing a lead for inhibitor development against human ACCs... - The Myxococcus xanthus wbgB gene encodes a glycosyltransferase homologue required for lipopolysaccharide O-antigen biosynthesisZ Yang
Department of Biological Sciences, Auburn University, AL 36849, USA
Arch Microbiol 174:399-405. 2000..xanthus cells. The pleiotrophic effects of wbgB mutations indicate the importance of LPS O-antigen biosynthesis for various cellular functions in M. xanthus... - Crystal structure of human Taspase1, a crucial protease regulating the function of MLLJaved A Khan
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Structure 13:1443-52. 2005..The structure unexpectedly showed the binding of a chloride ion in the active site, and our kinetic studies confirm that chlorides ions are inhibitors of this enzyme at physiologically relevant concentrations... - Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discoveryJaved A Khan
Columbia University, Department of Biological Sciences, New York, NY 10027, USA
Expert Opin Ther Targets 11:695-705. 2007..This review summarizes the existing knowledge on NAD(+) metabolic enzymes, with emphasis on their relevance for drug discovery... - Inhibition of p38 MAP kinase by utilizing a novel allosteric binding siteChristopher Pargellis
Department of Biology, Boehringer Ingelheim Pharmaceuticals, Research and Development Center, 900 Ridgebury Road, Ridgefield, Connecticut 06877, USA
Nat Struct Biol 9:268-72. 2002..One of the most potent compounds in this series, BIRB 796, has picomolar affinity for the kinase and low nanomolar inhibitory activity in cell culture... 
Crystal structures of respiratory pathogen neuraminidasesYu Shan Hsiao
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Biochem Biophys Res Commun 380:467-71. 2009..This work represents an important step in the development of drugs to prevent respiratory tract colonization by these two pathogens...- A different mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by tepraloxydimSong Xiang
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Proc Natl Acad Sci U S A 106:20723-7. 2009..Despite the chemical diversity between haloxyfop and tepraloxydim, the compounds do share two binding interactions to the enzyme, which may be important anchoring points for the development of ACC inhibitors... - Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reactionSong Xiang
Department of Biological Sciences, 212 Amsterdam Avenue, Columbia University, New York, New York 10027, USA
Nat Struct Mol Biol 15:295-302. 2008..There are dramatic differences in domain positions in the monomer and the organization of the tetramer between these enzymes and the PC from Rhizobium etli... - Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferaseFarhad Forouhar
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, New York 10027, USA
J Biol Chem 280:40328-36. 2005..In addition to preventing toxicity due to polyamine excess, this function may also serve to regulate expression of certain bacterial gene products such as those involved in sporulation... - Biochemical and functional studies on the regulation of the Saccharomyces cerevisiae AMPK homolog SNF1Gabriele A Amodeo
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Biochem Biophys Res Commun 397:197-201. 2010..This suggests that residues 450-500 may be constitutively associated with Snf4, and the remaining segments of the RS, as well as the AID, may be involved in regulating SNF1 activity... - A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme ALinda P C Yu
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Structure 17:823-32. 2009..Our structural information suggests that acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of PC that might be catalytically more competent... - Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylaseChristine S Huang
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Nature 466:1001-5. 2010.... - The use of in situ proteolysis in the crystallization of murine CstF-77Yun Bai
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Acta Crystallogr Sect F Struct Biol Cryst Commun 63:135-8. 2007..After an extensive search, it was found that 55% glucose can be used as a cryoprotectant while maintaining the diffraction quality of the crystals; most other commonly used cryoprotectants were detrimental to the diffraction quality... - Crystal structure of AGR_C_4470p from Agrobacterium tumefaciensSergey M Vorobiev
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, New York 10027, USA
Protein Sci 16:535-8. 2007..This is supported by the presence of two homologs of AGR_C_4470p in E. coli, in addition to the ChuS protein... - Crystal structure of murine CstF-77: dimeric association and implications for polyadenylation of mRNA precursorsYun Bai
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Mol Cell 25:863-75. 2007..The mode of dimerization and the relative arrangement of the HAT-N and HAT-C domains are unique to CstF-77. Our data support a role for CstF dimerization in pre-mRNA 3' end processing... - Structural evidence for direct interactions between the BRCT domains of human BRCA1 and a phospho-peptide from human ACC1Yang Shen
Department of Biological Sciences, Columbia University, New York City, New York 10027, USA
Biochemistry 47:5767-73. 2008..Our studies establish a framework for understanding the regulation of lipid biosynthesis by BRCA1 through its inhibition of ACC1 activity, which could be a novel tumor suppressor function of BRCA1... - Functional insights from structural genomicsFarhad Forouhar
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA
J Struct Funct Genomics 8:37-44. 2007..coli EutN), a proline racemase homolog with a disrupted active site (B. melitensis BME11586), an FMN-dependent enzyme (S. pneumoniae SP_1951), and a 12-stranded beta-barrel with a novel fold (V. parahaemolyticus VPA1032)... - Structural and functional studies of the abundant tegument protein ORF52 from murine gammaherpesvirus 68Jordi Benach
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, New York 10027, USA
J Biol Chem 282:31534-41. 2007..The results of the functional studies are fully consistent with the structural observations and indicate that the N-terminal alpha-helix is a crucial site of interaction for ORF52... - Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenaseFarhad Forouhar
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA
Proc Natl Acad Sci U S A 104:473-8. 2007..The active site is completely devoid of water during catalysis, which is supported by our electrochemical studies showing significant stabilization of the enzyme upon substrate binding... - Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in complex with CP-640186Hailong Zhang
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Structure 12:1683-91. 2004..The affinity of inhibitors for the CT domain has been assessed using kinetic and fluorescence anisotropy binding studies. The structural information identifies three regions for drug binding in the active site of CT... - A novel NAD-binding protein revealed by the crystal structure of 2,3-diketo-L-gulonate reductase (YiaK)Farhad Forouhar
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA
J Biol Chem 279:13148-55. 2004..The free enzyme conformation is incompatible with NAD binding. His(44) is likely the catalytic residue of the enzyme... - Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMPGerwald Jogl
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Biochemistry 43:1425-31. 2004..A rotation of 140 degrees in the small domain is needed for the binding of CoA and the catalysis of the second step. In contrast to the monomeric bacterial enzyme, yeast ACS is a stable trimer... - Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferaseYu Shan Hsiao
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
J Biol Chem 279:31584-9. 2004..8-A resolution. The F565A mutation has minor effects on the structure or the substrate preference of the enzyme... - Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolutionGerwald Jogl
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Proc Natl Acad Sci U S A 100:50-5. 2003.... - Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643Zhiru Yang
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
J Biol Chem 278:8804-8. 2003..Therefore, our studies demonstrate that two different enzymes, an oxidase and a dehydrogenase, may have evolved to catalyze the first step of NAD biosynthesis in prokaryotes. TM1643 establishes a new class of amino acid dehydrogenases... - An extensively associated dimer in the structure of the C713S mutant of the TIR domain of human TLR2Xiao Tao
Department of Biological Sciences, Columbia University, 10027, New York, NY, USA
Biochem Biophys Res Commun 299:216-21. 2002..Moreover, the structure shows that the BB loop can adopt different conformations, which are required for the formation of this dimer. This asymmetric dimer might represent the TLR2:TLRx heterodimer in the function of this receptor... - Crystal structures of MTH1187 and its yeast ortholog YBL001cXiao Tao
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, New York 10027, USA
Proteins 52:478-80. 2003 - Structural studies of the pigeon cytosolic NADP(+)-dependent malic enzymeZhiru Yang
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Protein Sci 11:332-41. 2002..Our structural studies also revealed differences in the organization of the tetramer between the pigeon and the human enzymes, although the pigeon enzyme still obeys 222 symmetry... - Characterization of the monomer-dimer equilibrium of human cytomegalovirus protease by kinetic methodsReza Khayat
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Biochemistry 43:316-22. 2004..5 M Na2SO4), respectively. Detailed kinetic analysis also showed that, in addition to the 260-fold stabilization of the dimer, the anti-chaotropic agents produced a 7-fold enhancement in the catalytic activity of the dimer... - Crystal structure of human nicotinamide riboside kinaseJaved A Khan
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Structure 15:1005-13. 2007..Mutation of residues in the active site can abolish the catalytic activity of the enzyme, confirming the structural observations... - Conserved surface features form the double-stranded RNA binding site of non-structural protein 1 (NS1) from influenza A and B virusesCuifeng Yin
Center for Advanced Biotechnology and Medicine, Northeast Structural Genomics Consortium, Department of Molecular Biology and Biochemistry, Robert Wood Johnson Medical School, Rutgers University, Piscataway, NJ 08854, USA
J Biol Chem 282:20584-92. 2007..This pocket provides a target on the surface of the NS1 protein that is potentially suitable for the development of antiviral drugs targeting both influenza A and B viruses... - Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transportGerwald Jogl
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Cell 112:113-22. 2003..Specifically, our structural information suggests that the substrate carnitine may assist the catalysis by stabilizing the oxyanion in the reaction intermediate... - How to get all "A"s in polyadenylationCorey R Mandel
Structure 15:1024-6. 2007.... - Molecular insights into the biosynthesis of the F420 coenzymeFarhad Forouhar
Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, New York 10027, USA
J Biol Chem 283:11832-40. 2008..Large structural differences in the active site region of the non-F(420)-producing CofD homologs suggest that they catalyze a different biochemical reaction... - Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domainGerwald Jogl
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
EMBO J 21:4785-95. 2002..Functional studies in intact cells demonstrate the requirement of both the PH and the BEACH domains for activity. A prominent groove at the interface between the two domains may be used to recruit their binding partners... - Crystal structure of human DJ-1, a protein associated with early onset Parkinson's diseaseXiao Tao
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
J Biol Chem 278:31372-9. 2003..The DJ-1 proteins may function only as dimers. The Lys to Arg mutation at residue 130, the site of sumoylation of DJ-1, has minimal impact on the structure of the protein... - Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5Xiao Tao
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Protein Sci 16:880-6. 2007..The CD of MKP5 is observed in an active conformation, and two loops in the active site have backbone shifts of up to 5 A relative to the inactive CDs from other MKPs... - Crystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivityGerwald Jogl
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
J Biol Chem 280:738-44. 2005..The side chains of Cys-323 and Met-335 at the bottom of this pocket assume dual conformations in the substrate complex, and mutagenesis studies suggest that the Met-335 residue is important for catalysis... - Crystal structure of the PH-BEACH domains of human LRBA/BGLDamara Gebauer
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Biochemistry 43:14873-80. 2004..The structure suggests intimate association between the PH and the BEACH domains, and surface plasmon resonance studies confirm that the two domains of the protein FAN have high affinity for each other, with a K(d) of 120 nM... - Structural and biochemical studies of inhibitor binding to human cytomegalovirus proteaseReza Khayat
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Biochemistry 42:885-91. 2003..Favorable and stereospecific interactions have been established in the S(1)' pocket for one of these inhibitors... - Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channelsYu hang Chen
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Nature 429:675-80. 2004..The presence of multiple protein-interacting modules in the beta-subunit opens a new dimension to its function as a multi-functional protein... - Engineering d-amino acid containing novel protease inhibitors using catalytic site architectureSubhash C Annedi
Molecular Design and Information Technology Center, Leslie Dan Faculty of Pharmacy, University of Toronto, Toronto, Canada ON M5S 2S2
Bioorg Med Chem 14:214-36. 2006..More potent and specific inhibitors could be designed with structure optimization as this strategy is completely general and can be used to design inhibitors against any serine or cysteine protease... - Molecular basis for the inhibition of human NMPRTase, a novel target for anticancer agentsJaved A Khan
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
Nat Struct Mol Biol 13:582-8. 2006..Contrary to current knowledge, the structures show that FK866 should compete directly with the nicotinamide substrate. Our structural and biochemical studies provide a starting point for the development of new anticancer agents... - Crystal structures of murine carnitine acetyltransferase in ternary complexes with its substratesYu Shan Hsiao
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
J Biol Chem 281:28480-7. 2006..The structural information provides significant new insights into the catalytic mechanism of CrAT and possibly carnitine acyltransferases in general... - Metal-Induced reversible structural interconversion of human mitochondrial NAD(P)+-dependent malic enzymeChu-Wei Kuo
Institute of Biochemistry, National Defense Medical Center, Taipei, Taiwan
Proteins 54:404-11. 2004..Excess Mn2+ could replace Lu3+ in the metal binding site and convert the inactive form back into the open form. This reversible process was slow in both directions because of the same but opposite structural change involved... - Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesisSong Xiang
Department of Biological Sciences, Columbia University, New York, New York 10027, USA
J Biol Chem 282:2676-82. 2007..The structures identify residues that may have important roles in catalysis, which have been confirmed by our mutagenesis studies... - Functional and structural basis of carnitine palmitoyltransferase 1A deficiencyStephanie Gobin
Departement d Endocrinologie, Institut Cochin, INSERM U567, CNRS Unité Mixte de Recherche 8104, Universite Rene Descartes, 24 rue du Faubourg Saint Jacques, 75014 Paris, France
J Biol Chem 278:50428-34. 2003..This study provides novel insights into the functionality of CPT1A that may contribute to the design of drugs for the treatment of lipid disorders... - Novel homozygous p.E64D mutation in DJ1 in early onset Parkinson disease (PARK7)Robert Hering
Department of Medical Genetics, University of Tubingen, Tubingen, Germany
Hum Mutat 24:321-9. 2004.... - Structure of the Bateman2 domain of yeast Snf4: dimeric association and relevance for AMP bindingMichael J Rudolph
Department of Biological Sciences, Columbia University, New York, NY 10027, USA
Structure 15:65-74. 2007..There is a prominent pocket at the center of this dimer, and most of the disease-causing mutations are located in or near this pocket...