Abstract: We have also solved crystal structures of two multi-drug resistant mutant HIV PRs in complex with TL-3, from subtype B (Bmut) carrying the primary mutations V82A and L90M, and from subtype F (Fmut) carrying the primary mutation V82A plus the secondary mutation M36I, at 1.75 A and 2.8 A resolution, respectively.
HIV-1 subtype B protease and reverse transcriptase amino acid covariation.
Abstract: Patterns of protease covariation were dominated by the clustering of nelfinavir-associated mutations (D30N and N88D), two main groups of protease inhibitor (PI)-resistance mutations associated either with V82A or L90M, and a tight cluster of mutations associated with decreased susceptibility to amprenavir and the most recently approved PI darunavir.
Discussion: Protease covariation was dominated by the clustering of nelfinavir-associated mutations (D30N and N88D), two main groups of PI-resistance mutations associated either with V82A
X-ray crystal structures of human immunodeficiency virus type 1 protease mutants complexed with atazanavir.
Abstract: This work describes the X-ray crystal structures of complexes of atazanavir with two HIV-1 protease variants, namely, (i) an enzyme optimized for resistance to autolysis and oxidation, referred to as the cleavage-resistant mutant (CRM); and (ii) the M46I/V82F/I84V/L90M mutant of the CRM enzyme, which is resistant to all approved HIV-1 protease inhibitors, referred to as the inhibitor-resistant mutant.
Insight into analysis of interactions of saquinavir with HIV-1 protease in comparison between the wild-type and G48V and G48V/L90M mutants based on QM and QM/MM calculations.
PMID: 17543558
2007
Journal of molecular graphics & modelling
Abstract: Moreover, the G48V/L90M mutations cause the repositioning of the residues close to residues 48 and 90, at important locations as a part of the flap and catalytic regions, respectively.
Abstract: The two most important HIV-1 PR mutants are G48V and G48V/L90M.
Abstract: We have found that the interaction of SQV with flap residue 48 of the mutants is significantly perturbed, as shown by the reduced stability of binding between SQV and residue 48 for the G48V and G48V/L90M mutants over the wild-type.
Changing rates and patterns of drug resistance mutations in antiretroviral-experienced HIV-infected patients.
PMID: 17678470
2007
AIDS research and human retroviruses
Abstract: The most frequent PI resistance mutations were L90M (24.3%), V82X (19.9%), M46I/L (19.5%), and I54V (17.1%).
Mutational patterns and correlated amino acid substitutions in the HIV-1 protease after virological failure to nelfinavir- and lopinavir/ritonavir-based treatments.
Abstract: A series of correlated mutations including L10I, M46I, I54V, A71V, G73S, and L90M appeared as a common cluster of amino acid substitutions, associated with failure to lopinavir/ritonavir-based treatments.
Abstract: On the other hand, L90M together with L10I, I54V, A71V, G73S, and V82A were selected in protease inhibitor-experienced patients.
Genotype testing and antiretroviral resistance profiles from HIV-1 patients experiencing therapeutic failure in northeast Brazil.
PMID: 17873990
2007
The Brazilian journal of infectious diseases
Abstract: The most frequent mutations were: L90M, M184V and K103N related to PI's, NRTI's and NNRTI's, respectively.
Impact of the number of failed therapeutic regimes on the development of resistance mutations to HIV-1 in northeast Brazil.
PMID: 17962868
2007
The Brazilian journal of infectious diseases
Abstract: There was a significant increase in resistance mutations V82A/F/L/T, I84V, L90M, M41L, K70R, L210W, T215Y/F and K219Q/E in MF.
Molecular analysis of the HIV-1 resistance development: enzymatic activities, crystal structures, and thermodynamics of nelfinavir-resistant HIV protease mutants.
Abstract: Crystal structures, molecular dynamics simulations, and calorimetric data for four mutants (D30N, D30N/A71V, D30N/N88D, and D30N/L90M) were used to augment our kinetic data.
Abstract: Here we analyze the proteolytic activities, X-ray structures, and thermodynamics of inhibitor binding to HIV-1 PRs harboring the D30N and L90M mutations alone and in combination with other compensatory mutations.
Abstract: In the PR sequence of viral variants resistant to the PI nelfinavir, the mutations D30N and L90M
Insights into a mutation-assisted lateral drug escape mechanism from the HIV-1 protease active site.
Abstract: We provide insight into the first stages of a kinetic mechanism of lateral drug expulsion from the active site of HIV-1 protease, by conducting all atom molecular dynamics simulations with explicit solvent over a time scale of 24 ns for saquinavir bound to the wildtype, G48V, L90M and G48V/L90M mutant proteases.
HIV mutation literature information.
PMID: 
2007
Journal of molecular biology
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