Article
Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 angstroms resolution crystal structures of HIV-1 protease mutants with substrate analogs.
The FEBS journal - 1 Oct 2005
Tie Yunfeng, Boross Peter I, Wang Yuan-Fang, Gaddis Laquasha, Liu Fengling, Chen Xianfeng, Tozser Jozsef, Harrison Robert W, Weber Irene T
Abstract excerpt
HIV-1 protease (PR) and two drug-resistant variants--PR with the V82A mutation (PR(V82A)) and PR with the I84V mutation (PR(I84V))--were studied using reduced peptide analogs of five natural cleavage sites (CA-p2, p2-NC, p6pol-PR, p1-p6 and NC-p1) to understand the structural and kinetic changes. The common drug-resistant mutations V82A and I84V alter residues forming the substrate-binding site. Eight crystal...
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