Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
Here we report the X-ray structures of chemically synthesized HIV-1 protease and the inactive [D25N]HIV-1 protease complexed with the ketomethylene isostere inhibitor Ac-Thr-Ile-Nle psi[CO-CH(2)]Nle-Gln-Arg.amide at 1.4 and 1.8A resolution, respectively. In complex with the active enzyme, the keto-group was found to be converted into the hydrated gem-diol, while the structure of the complex with the inactive D25N enzyme revealed an intact keto-group. These data support the general acid-general base mechanism for HIV-1 protease catalysis.
Crystal structure of chemically synthesized HIV-1 protease and a ketomethylene isostere inhibitor based on the p2/NC cleavage site.,Torbeev VY, Mandal K, Terechko VA, Kent SB Bioorg Med Chem Lett. 2008 Aug 15;18(16):4554-7. Epub 2008 Jul 15. PMID:18657969[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Torbeev VY, Mandal K, Terechko VA, Kent SB. Crystal structure of chemically synthesized HIV-1 protease and a ketomethylene isostere inhibitor based on the p2/NC cleavage site. Bioorg Med Chem Lett. 2008 Aug 15;18(16):4554-7. Epub 2008 Jul 15. PMID:18657969 doi:http://dx.doi.org/10.1016/j.bmcl.2008.07.039
