The active site of HIV-1 protease

Authors
Citation
Pp. Mager, The active site of HIV-1 protease, MED RES REV, 21(4), 2001, pp. 348-353
Citations number
17
Categorie Soggetti
Pharmacology & Toxicology
Journal title
MEDICINAL RESEARCH REVIEWS
ISSN journal
01986325 → ACNP
Volume
21
Issue
4
Year of publication
2001
Pages
348 - 353
Database
ISI
SICI code
0198-6325(200107)21:4<348:TASOHP>2.0.ZU;2-J
Abstract
The active site of the homodimeric HIV-1 protease includes six amino acids (triads AspThrGly found in each monomer) in amino acid positions 25 to 27 a nd 25 ' to 27 '. Up to now, the role of Thr26 and Thr26 ', and Gly27 and Gl y27 ', is unknown. It is hypothesized that strong hydrogen-bonding forces b etween the Thr26 and Thr26 ' residues stabilize the conformational state of the active site, and that the function of Gly27 and Gly27 ' is to accommod ate and bind a substrate in a position in which the catalytic Asp25 and Asp 25 ' carboxylate groups can attack the amide moiety of a substrate. (C) 200 1 John Wiley & Sons, Inc.