Báo cáo khoa học: Molecular basis for substrate recognition and drug ˚ resistance from 1.1 to 1.6 A resolution crystal structures of HIV-1 protease mutants with substrate analogs
HIV-1 protease (PR) and two drug-resistant variants – PR with the V82A
mutation (PRV82A) and PR with the I84V mutation (PRI84V) – were studied
using reduced peptide analogs of five natural cleavage sites (CA-p2,
p2-NC, p6
pol
-PR, p1-p6 and NC-p1) to understand the structural and kine-tic changes. The common drug-resistant mutations V82A and I84V alter
residues forming the substrate-binding site. Eight crystal structures were
refined at resolutions of 1.10–1.60 A
˚
.
