Abstract: The active-site expansion includes position 82 and 84 mutations due to the alterations in the amino acid side chains from longer to shorter (e.g., V82A and I84V).
A Comparative Insight into Amprenavir Resistance of Mutations V32I, G48V, I50V, I54V, and I84V in HIV-1 Protease Based on Thermodynamic Integration and MM-PBSA Methods.
Abstract: Consequently, this study examined structural properties sampled during 22 nsec, all atom molecular dynamics (MD) simulations (in explicit water) of both a wild-type and the drug-resistant V82F/I84V mutant of HIV-1 protease.
Abstract: The V82F/I84V mutation significantly decreases the binding affinity of all HIV-1 protease inhibitors currently used clinically.
High resolution crystal structures of HIV-1 protease with a potent non-peptide inhibitor (UIC-94017) active against multi-drug-resistant clinical strains.
Abstract: The crystal structures of PR and PR(I84V) with UIC-94017 ternary complexes show that the inhibitor binds to the protease in two overlapping positions, while the PR(V82A) complex had one ordered inhibitor.
Abstract: We have determined the high-resolution crystal structures of UIC-94017 in complexes with wild-type HIV-1 protease (PR) and mutant proteases PR(V82A) and PR(I84V) that are common in drug-resistant HIV.
HIV protease mutations associated with amprenavir resistance during salvage therapy: importance of I54M.
Abstract: The V82F/I84V double mutation is located within the binding site cavity and affects all protease inhibitors in clinical use.
Abstract: The structures of the two compounds bound to the wild type and V82F/I84V HIV-1 protease have been determined by X-ray crystallography at 2.0 A resolution.
Mutation D30N is not preferentially selected by human immunodeficiency virus type 1 subtype C in the development of resistance to nelfinavir.
PMID: 15155216
2004
Antimicrobial agents and chemotherapy
Abstract: Other mutations were L10I/V, K20R, M46I, V82A/I, I84V, N88D, and N88S.
Persistence of mutations during replication of an HIV library containing combinations of selected protease mutations.
Abstract: However, the mutations M36I, M46I and I84V were relatively persistent: t(1/2) = 34.2, 28.1 and 30.6 days, respectively.
Resistance profiles observed in virological failures after 24 weeks of amprenavir/ritonavir containing regimen in protease inhibitor experienced patients.
Abstract: Among these patients, the selection of mutations previously described with the use of APV as first PI (V32I, L33F, M46I/L, I50V, 54M/L, and I84V) was observed.
Abstract: Several genotypic resistance pathways in protease gene have been described to be associated to unboosted APV failure (I50V, V32I + I47V, I54L/M, or less commonly I84V, which may be accompanied by one ore more accessory mutations such as L10F, L33F, M46I/L).
Comparing the accumulation of active- and nonactive-site mutations in the HIV-1 protease.
Abstract: To examine the basis for this potency, we solved crystal structures of TMC114 complexed with wt HIV-1 protease and TMC114 and APV complexed with an MDR (L63P, V82T, and I84V) protease variant.
HIV mutation literature information.
PMID: 
2004
Journal of virology
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