|
Basic Characteristics of Mutations
|
|
Mutation Site
|
I13V |
|
Mutation Site Sentence
|
This result is in alignment with other reports, where the polymorphic mutation I13V was linked with the mutation of Thr to Ala at the P3 position of the natural cleavage site p24/p2. |
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Mutation Level
|
Amino acid level |
|
Mutation Type
|
Nonsynonymous substitution |
|
Gene/Protein/Region
|
PR |
|
Standardized Encoding Gene
|
gag-pol
|
|
Genotype/Subtype
|
HIV-1;HIV-2 |
|
Viral Reference
|
K03455.1
|
|
Functional Impact and Mechanisms
|
|
Disease
|
-
|
|
Immune
|
- |
|
Target Gene
|
-
|
|
Clinical and Epidemiological Correlations
|
|
Clinical Information
|
- |
|
Treatment
|
- |
|
Location
|
- |
|
Literature Information
|
|
PMID
|
17352531
|
|
Title
|
A look inside HIV resistance through retroviral protease interaction maps
|
|
Author
|
Kontijevskis A,Prusis P,Petrovska R,Yahorava S,Mutulis F,Mutule I,Komorowski J,Wikberg JE
|
|
Journal
|
PLoS computational biology
|
|
Journal Info
|
2007 Mar 9;3(3):e48
|
|
Abstract
|
Retroviruses affect a large number of species, from fish and birds to mammals and humans, with global socioeconomic negative impacts. Here the authors report and experimentally validate a novel approach for the analysis of the molecular networks that are involved in the recognition of substrates by retroviral proteases. Using multivariate analysis of the sequence-based physiochemical descriptions of 61 retroviral proteases comprising wild-type proteases, natural mutants, and drug-resistant forms of proteases from nine different viral species in relation to their ability to cleave 299 substrates, the authors mapped the physicochemical properties and cross-dependencies of the amino acids of the proteases and their substrates, which revealed a complex molecular interaction network of substrate recognition and cleavage. The approach allowed a detailed analysis of the molecular-chemical mechanisms involved in substrate cleavage by retroviral proteases.
|
|
Sequence Data
|
-
|