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Basic Characteristics of Mutations
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Mutation Site
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A71V |
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Mutation Site Sentence
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The active site pocket, and G48V and I54V in the flap regions, non-active site mutations L90M and A71V may indirectly influence inhibitor or substrate binding. |
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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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HIV Infections
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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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PIs |
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Location
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- |
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Literature Information
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PMID
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27039930
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Title
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Binding of Clinical Inhibitors to a Model Precursor of a Rationally Selected Multidrug Resistant HIV-1 Protease Is Significantly Weaker Than That to the Released Mature Enzyme
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Author
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Park JH,Sayer JM,Aniana A,Yu X,Weber IT,Harrison RW,Louis JM
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Journal
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Biochemistry
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Journal Info
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2016 Apr 26;55(16):2390-400
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Abstract
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We have systematically validated the activity and inhibition of a HIV-1 protease (PR) variant bearing 17 mutations (PR(S17)), selected to represent high resistance by machine learning on genotype-phenotype data. Three of five mutations in PR(S17) correlating with major drug resistance, M46L, G48V, and V82S, and five of 11 natural variations differ from the mutations in two clinically derived extreme mutants, PR20 and PR22 bearing 19 and 22 mutations, respectively. PR(S17), which forms a stable dimer (<10 nM), is approximately 10- and 2-fold less efficient in processing the Gag polyprotein than the wild type and PR20, respectively, but maintains the same cleavage order. Isolation of a model precursor of PR(S17) flanked by the 56-amino acid transframe region (TFP-p6pol) at its N-terminus, which is impossible upon expression of an analogous PR20 precursor, allowed systematic comparison of inhibition of TFP-p6pol-PR(S17) and mature PR(S17). Resistance of PR(S17) to eight protease inhibitors (PIs) relative to PR (Ki) increases by 1.5-5 orders of magnitude from 0.01 to 8.4 muM. Amprenavir, darunavir, atazanavir, and lopinavir, the most effective of the eight PIs, inhibit precursor autoprocessing at the p6pol/PR site with IC50 values ranging from approximately 7.5 to 60 muM. Thus, this process, crucial for stable dimer formation, shows inhibition approximately 200-800-fold weaker than that of the mature PR(S17). TFP/p6pol cleavage, which occurs faster, is inhibited even more weakly by all PIs except darunavir (IC50 = 15 muM); amprenavir shows a 2-fold increase in IC50 ( approximately 15 muM), and atazanavir and lopinavir show increased IC50 values of >42 and >70 muM, respectively.
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Sequence Data
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-
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