Review
doi: 10.1002/med.1012.
The active site of HIV-1 protease
Affiliations
- PMID: 11410934
- DOI: 10.1002/med.1012
Item in Clipboard
Review
The active site of HIV-1 protease
Med Res Rev.
2001 Jul.
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 and 25' to 27'. Up to now, the role of Thr26 and Thr26', and Gly27 and Gly27', is unknown. It is hypothesized that strong hydrogen-bonding forces between the Thr26 and Thr26' residues stabilize the conformational state of the active site, and that the function of Gly27 and Gly27' is to accommodate and bind a substrate in a position in which the catalytic Asp25 and Asp25' carboxylate groups can attack the amide moiety of a substrate.
Copyright 2001 John Wiley & Sons, Inc. Med Res Rev, 21, No. 4, 348-353, 2001
Similar articles
-
Interactions of the dimeric triad of HIV-1 aspartyl protease with inhibitors.Drug Des Discov. 2003;18(2-3):53-64. Drug Des Discov. 2003. PMID: 14675943
-
Ionization state of the catalytic dyad Asp25/25' in the HIV-1 protease: NMR studies of site-specifically 13C labelled HIV-1 protease prepared by total chemical synthesis.Org Biomol Chem. 2012 Aug 14;10(30):5887-91. doi: 10.1039/c2ob25569c. Epub 2012 Jun 1. Org Biomol Chem. 2012. PMID: 22659831 Free PMC article.
-
A density functional study of the hydrogen-bond network within the HIV-1 protease catalytic site cleft.J Comput Chem. 2003 Jul 15;24(9):1110-9. doi: 10.1002/jcc.10176. J Comput Chem. 2003. PMID: 12759910
-
Design of symmetry-based, peptidomimetic inhibitors of human immunodeficiency virus protease.Methods Enzymol. 1994;241:334-54. doi: 10.1016/0076-6879(94)41072-0. Methods Enzymol. 1994. PMID: 7854187 Review. No abstract available.
-
Design of tight-binding human immunodeficiency virus type 1 protease inhibitors.Methods Enzymol. 1994;241:311-34. doi: 10.1016/0076-6879(94)41071-2. Methods Enzymol. 1994. PMID: 7854186 Review. No abstract available.
Cited by
-
Interdependence of Inhibitor Recognition in HIV-1 Protease.J Chem Theory Comput. 2017 May 9;13(5):2300-2309. doi: 10.1021/acs.jctc.6b01262. Epub 2017 Apr 11. J Chem Theory Comput. 2017. PMID: 28358514 Free PMC article.
-
Whiskers-less HIV-protease: a possible way for HIV-1 deactivation.J Biomed Sci. 2013 Sep 12;20(1):67. doi: 10.1186/1423-0127-20-67. J Biomed Sci. 2013. PMID: 24024748 Free PMC article.
-
Cellular Targets of HIV-1 Protease: Just the Tip of the Iceberg?Viruses. 2023 Mar 9;15(3):712. doi: 10.3390/v15030712. Viruses. 2023. PMID: 36992421 Free PMC article. Review.
-
OPUS-Mut: Studying the Effect of Protein Mutation through Side-Chain Modeling.J Chem Theory Comput. 2023 Mar 14;19(5):1629-1640. doi: 10.1021/acs.jctc.2c00847. Epub 2023 Feb 22. J Chem Theory Comput. 2023. PMID: 36813264 Free PMC article.
-
Conformational Variation in Enzyme Catalysis: A Structural Study on Catalytic Residues.J Mol Biol. 2022 Apr 15;434(7):167517. doi: 10.1016/j.jmb.2022.167517. Epub 2022 Feb 28. J Mol Biol. 2022. PMID: 35240125 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
