|
Basic Characteristics of Mutations
|
|
Mutation Site
|
K45A |
|
Mutation Site Sentence
|
Table 5. Strategy2 suggested mutant PRs |
|
Mutation Level
|
Amino acid level |
|
Mutation Type
|
Nonsynonymous substitution |
|
Gene/Protein/Region
|
PR |
|
Standardized Encoding Gene
|
gag-pol
|
|
Genotype/Subtype
|
HIV-1 |
|
Viral Reference
|
-
|
|
Functional Impact and Mechanisms
|
|
Disease
|
-
|
|
Immune
|
- |
|
Target Gene
|
-
|
|
Clinical and Epidemiological Correlations
|
|
Clinical Information
|
- |
|
Treatment
|
PIs |
|
Location
|
- |
|
Literature Information
|
|
PMID
|
24796579
|
|
Title
|
In silico prediction of mutant HIV-1 proteases cleaving a target sequence
|
|
Author
|
Jensen JH,Willemoes M,Winther JR,De Vico L
|
|
Journal
|
PloS one
|
|
Journal Info
|
2014 May 5;9(5):e95833
|
|
Abstract
|
HIV-1 protease represents an appealing system for directed enzyme re-design, since it has various different endogenous targets, a relatively simple structure and it is well studied. Recently Chaudhury and Gray (Structure (2009) 17: 1636-1648) published a computational algorithm to discern the specificity determining residues of HIV-1 protease. In this paper we present two computational tools aimed at re-designing HIV-1 protease, derived from the algorithm of Chaudhuri and Gray. First, we present an energy-only based methodology to discriminate cleavable and non cleavable peptides for HIV-1 proteases, both wild type and mutant. Secondly, we show an algorithm we developed to predict mutant HIV-1 proteases capable of cleaving a new target substrate peptide, different from the natural targets of HIV-1 protease. The obtained in silico mutant enzymes were analyzed in terms of cleavability and specificity towards the target peptide using the energy-only methodology. We found two mutant proteases as best candidates for specificity and cleavability towards the target sequence.
|
|
Sequence Data
|
-
|