| Literature DB >> 20953192 |
Lisa M Miller Jenkins1, David E Ott, Ryo Hayashi, Lori V Coren, Deyun Wang, Qun Xu, Marco L Schito, John K Inman, Daniel H Appella, Ettore Appella.
Abstract
The zinc fingers of the HIV-1 nucleocapsid protein, NCp7, are prime targets for antiretroviral therapeutics. Here we show that S-acyl-2-mercaptobenzamide thioester (SAMT) chemotypes inhibit HIV by modifying the NCp7 region of Gag in infected cells, thereby blocking Gag processing and reducing infectivity. The thiol produced by SAMT reaction with NCp7 is acetylated by cellular enzymes to regenerate active SAMTs via a recycling mechanism unique among small-molecule inhibitors of HIV.Entities:
Mesh:
Substances:
Year: 2010 PMID: 20953192 PMCID: PMC2997617 DOI: 10.1038/nchembio.456
Source DB: PubMed Journal: Nat Chem Biol ISSN: 1552-4450 Impact factor: 15.040