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Review
. 1998 Nov;42(11):2775-83.
doi: 10.1128/AAC.42.11.2775.

Resistance to human immunodeficiency virus type 1 protease inhibitors

D Boden  1 , M Markowitz
Affiliations
Review

Resistance to human immunodeficiency virus type 1 protease inhibitors

D Boden et al. Antimicrob Agents Chemother. 1998 Nov.
No abstract available

PubMed Disclaimer

Figures

FIG. 1
FIG. 1
Schematic structure of HIV-1 protease. Active-site residues are yellow; residues in the flap region are red; residue 46 and the flap hinge are dark blue; residues adjacent to the active site are light blue; residues distant from the active site of the enzyme are purple. Designations consist of the wild-type amino acid followed by the residue number and one or more described substitutions observed during protease inhibitor therapy; for example, I84V is a valine-for-isoleucine substitution at residue 84 in the protease monomer. (Courtesy of John Erickson.)
FIG. 2
FIG. 2
Computer-generated model of HIV-1 protease-ritonavir complexes of wild-type HIV-1NL4-3 and the V82F/I84V double mutant. (A) Interaction between ritonavir and the protease at the S1′ subsite; (B) the same interactions at the S1′ binding subsite. I84V decreases the interaction with the Cβ group of the benzyl side chain of ritonavir, whereas V82F results in a severe spatial overlap with the phenyl ring of the inhibitor at the P1′ site. Note the effects of the double mutant on the van der Waals interactions between the enzyme and the inhibitor.
See this image and copyright information in PMC

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