Article
HIV-1 protease mutations and inhibitor modifications monitored on a series of complexes. Structural basis for the effect of the A71V mutation on the active site.
Journal of medicinal chemistry - 21 Sept 2006
Skalova Tereza, Dohnalek Jan, Duskova Jarmila, Petrokova Hana, Hradílek Martin, Soucek Milan, Konvalinka Jan, Hasek Jindrich
Abstract excerpt
Two new X-ray structures of an HIV-1 protease mutant (A71V, V82T, I84V) in complex with inhibitors SE and SQ, pseudotetrapeptide inhibitors with an acyclic S-hydroxyethylamine isostere, were determined. Comparison of eight structures exploring the binding of four similar inhibitors--SE, SQ (S-hydroxyethylamine isostere), OE (ethyleneamine), and QF34 (hydroxyethylene)--to wild-type and A71V/V82T/I84V HIV-1...
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