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• W2040319998 abstract "Abstract Crystallographic data show that various substrates of HIV protease occupy a remarkably uniform region within the binding site; this region has been termed the substrate envelope. It has been suggested that an inhibitor that fits within the substrate envelope should tend to evade viral resistance because a protease mutation that reduces the affinity of the inhibitor will also tend to reduce the affinity of substrate, and will hence decrease the activity of the enzyme. Accordingly, inhibitors that fit the substrate envelope better should be less susceptible to clinically observed resistant mutations, since these must also allow substrates to bind. The present study describes a quantitative measure of the volume of a bound inhibitor falling outside the substrate envelope, and observes that this quantity correlates with the inhibitor's losses in affinity to clinically relevant mutants. This measure may thus be useful as a penalty function in the design of robust HIV protease inhibitors. Proteins 2007. © 2007 Wiley‐Liss, Inc." @default.
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• W2040319998 date "2007-05-01" @default.
• W2040319998 modified "2023-10-17" @default.
• W2040319998 title "Evaluation of the substrate envelope hypothesis for inhibitors of HIV-1 protease" @default.
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• W2040319998 doi "https://doi.org/10.1002/prot.21431" @default.
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