Genomes and Genes
Affiliation: University of Virginia
- On the mechanism of autoinhibition of the RhoA-specific nucleotide exchange factor PDZRhoGEFMeiying Zheng
Department of Molecular Physiology and Biological Physics, University of Virginia, PO Box 800736, Charlottesville, Virginia, 22908 0736, USA
BMC Struct Biol 9:36. 2009..These GEFs include p115, LARG and PDZRhoGEF (PRG)...
- The crystal structure of a major dust mite allergen Der p 2, and its biological implicationsU Derewenda
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA
J Mol Biol 318:189-97. 2002..The crystal structure suggests that binding of non-polar molecules may be essential to the physiological function of the Der p 2 protein...
- Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase IbP J Sheffield
Department of Molecular Physiology and Biological Physics, University of Virginia Health Sciences Center, Charlottesville, VA 22906 0011, USA
Protein Eng 14:513-9. 2001..The alpha(1)/alpha(2) dimer has been crystallized and its structure was solved at 2.1 A resolution by molecular replacement. These results set the stage for a detailed characterization of the PAF-AH Ib complex...
- Sequence polymorphisms and antibody binding to the group 2 dust mite allergensA M Smith
Asthma and Allergic Diseases Center, University of Virginia, Charlottesville, VA 22908 1355, USA
Int Arch Allergy Immunol 124:61-3. 2001..Isoforms within each genus have been identified which differ by 3-4 amino acids. The aim of this study was to investigate the importance of these substitutions to antibody binding...
- Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzymeJ Li
Department of Molecular Physiology and Biological Physics, University of Virginia, P O Box 800736, Charlottesville, Virginia 22908 0736, USA
Nat Struct Biol 7:555-9. 2000..The catalytic site, inferred from the crystal structure and verified by site directed mutagenesis, involves novel chemistry and includes Asp 204, Gln 278 and Thr 228, which synergistically activate a nucleophilic water molecule...
- How RhoGDI binds RhoK Longenecker
Department of Molecular Physiology and Biological Physics, University of Virginia Health Sciences Center, Charlottesville, VA 22906, USA
Acta Crystallogr D Biol Crystallogr 55:1503-15. 1999..The entrance of the hydrophobic pocket of RhoGDI is 25 A from the last residue in the RhoA model, with its C-terminus oriented to accommodate the geranylgeranyl group without conformational change in RhoA...
- Homologs of the alpha- and beta-subunits of mammalian brain platelet-activating factor acetylhydrolase Ib in the Drosophila melanogaster genomeP J Sheffield
Department of Molecular Physiology and Biological Physics, University of Virginia, Health Sciences Center, Charlottesville, Virginia 22908, USA
Proteins 39:1-8. 2000..Our study shows that the beta-subunit homolog is highly conserved from Drosophila to mammals and is able to interact with the mammalian alpha-subunits but is unable to interact with the Drosophila alpha-subunit. Proteins 2000;39:1-8...
- The molecular basis of antigenic cross-reactivity between the group 2 mite allergensA M Smith
Asthma and Allergic Diseases Center, Department of Medicine, University of Virginia Health System, Charlottesville, VA 22908-1355, USA
J Allergy Clin Immunol 107:977-84. 2001....
- Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimerY S Ho
Department of Molecular Physiology and Biological Physics, University of Virginia Health Sciences Center, Charlottesville 22906 0011, USA
Nature 385:89-93. 1997..The active site is made up of a trypsin-like triad of Ser 47, His 195 and Asp 192. Thus, the intact PAF-AH(Ib) molecule is an unusual G-protein-like (alpha1/alpha2)beta trimer...
- Cross-reactivity studies of a new group 2 allergen from the dust mite Glycyphagus domesticus, Gly d 2, and group 2 allergens from Dermatophagoides pteronyssinus, Lepidoglyphus destructor, and Tyrophagus putrescentiae with recombinant allergensG Gafvelin
Department of Medicine, Division of Clinical Immunology and Allergy, Karolinska Hospital and Institutet, Stockholm, Sweden
J Allergy Clin Immunol 107:511-8. 2001..CONCLUSION: Gly d 2 showed high sequence homology to Lep d 2. Cross-reactivity was observed between Gly d 2, Lep d 2, and Tyr p 2, but only limited cross-reactivity was demonstrated between these 3 allergens and Der p 2...
- Substrate specificity in glycoside hydrolase family 10. Structural and kinetic analysis of the Streptomyces lividans xylanase 10AV Ducros
Department of Chemistry, Structural Biology Laboratory, University of York, Heslington, York YO10 5DD, United Kingdom
J Biol Chem 275:23020-6. 2000....
- Crystal structure of RhoA-GDP and its functional implicationsY Wei
Nat Struct Biol 4:699-703. 1997..A 2.1 A resolution crystal structure of the human RhoA-GDP complex shows unique stereochemistry in the switch I region, which results in a novel mode of Mg2+ binding...
- Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanasesU Derewenda
Department of Biochemistry, University of Alberta, Edmonton, Canada
J Biol Chem 269:20811-4. 1994..The crystal structure supports the earlier assignment of Glu-128 and Glu-236 as the catalytic amino acids (Moreau, A., Roberge, M., Manin, C., Shareck, F., Kluepfel, D., and Morosoli, R. (1994) Biochem. J., in press)...