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Content Provider | World Health Organization (WHO)-Global Index Medicus |
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Author | Everitt, L. Manchester, M. Loeb, D. D. Shao, W. Hutchison, C. A. Swanstrom, R. |
Description | Author Affiliation: Shao W ( Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, 27599, USA.); |
Abstract | The retroviral proteases (PRs) have a structural feature called the flap, which consists of a short anti-parallel beta-sheet with a turn. The flap extends over the substrate binding cleft and must be flexible to allow entry and exit of the polypeptide substrates and products. We analyzed the sequence requirements of the amino acids within the flap region (positions 46-56) of the HIV-1 PR. The phenotypes of 131 substitution mutants were determined using a bacterial expression system. Four of the mutant PRs with mutations in different regions of the flap were selected for kinetic analysis. Our phenotypic analysis, considered in the context of published structures of the HIV-1 PR with a bound substrate analogs, shows that: (i) Met-46 and Phe-53 participate in hydrophobic interactions on the solvent-exposed face of the flap; (ii) Ile-47, Ile-54, and Val-56 participate in hydrophobic interactions on the inner face of the flap; (iii) Ile-50 has hydrophobic interactions at the distance of both the delta and gamma carbons; (iv) the three glycine residues in the beta-turn of the flap are virtually intolerant of substitutions. Among these mutant PRs, we have identified changes in both kcat and Km. These results establish the nature of the side chain requirements at each position in the flap and document a role for the flap in both substrate binding and catalysis. |
ISSN | 00278424 |
e-ISSN | 10916490 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Issue Number | 6 |
Volume Number | 94 |
Language | English |
Publisher | National Academy of Sciences |
Publisher Date | 1997-04-01 |
Publisher Place | United States |
Access Restriction | Open |
Subject Keyword | HIV Protease Chemistry Metabolism Protein Conformation Amino Acid Sequence Binding Sites Glycine HIV-1 Enzymology Isoleucine Kinetics Methionine Models, Molecular Mutagenesis, Site-Directed Phenylalanine Recombinant Proteins Solvents Valine Comparative Study Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
Content Type | Text |
Resource Type | Article |
Subject | Multidisciplinary |
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