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Basic Characteristics of Mutations
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Mutation Site
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V32I |
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Mutation Site Sentence
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Solution Kinetics Measurements Suggest HIV-1 Protease Has Two Binding Sites for Darunavir and AmprenavirDarunavir, a potent antiviral drug, showed an unusual second binding site on the HIV-1 protease dimer surface of the V32I drug resistant mutant and normal binding in the active site cavity. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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PR |
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Standardized Encoding Gene
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gag-pol
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Genotype/Subtype
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HIV-1 |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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-
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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Darunavir and Amprenavir |
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Location
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- |
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Literature Information
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PMID
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18808097
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Title
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Solution kinetics measurements suggest HIV-1 protease has two binding sites for darunavir and amprenavir
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Author
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Kovalevsky AY,Ghosh AK,Weber IT
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Journal
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Journal of medicinal chemistry
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Journal Info
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2008 Oct 23;51(20):6599-603
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Abstract
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Darunavir, a potent antiviral drug, showed an unusual second binding site on the HIV-1 protease dimer surface of the V32I drug resistant mutant and normal binding in the active site cavity. Kinetic analysis for wild type and mutant protease showed mixed-type competitive-uncompetitive inhibition for darunavir and the chemically related amprenavir, while saquinavir showed competitive inhibition. The inhibition model is consistent with the observed second binding site for darunavir and helps to explain its antiviral potency.
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Sequence Data
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-
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