|
Basic Characteristics of Mutations
|
|
Mutation Site
|
N239G |
|
Mutation Site Sentence
|
Results from the MD of N239G mutant. |
|
Mutation Level
|
Amino acid level |
|
Mutation Type
|
nonsynonymous substitution |
|
Gene/Protein/Region
|
gp120 |
|
Standardized Encoding Gene
|
Env
|
|
Genotype/Subtype
|
HIV-1 |
|
Viral Reference
|
-
|
|
Functional Impact and Mechanisms
|
|
Disease
|
-
|
|
Immune
|
- |
|
Target Gene
|
-
|
|
Clinical and Epidemiological Correlations
|
|
Clinical Information
|
- |
|
Treatment
|
gp120 |
|
Location
|
- |
|
Literature Information
|
|
PMID
|
33466381
|
|
Title
|
Does Antibody Stabilize the Ligand Binding in GP120 of HIV-1 Envelope Protein? Evidence from MD Simulation
|
|
Author
|
Yadav S,Pandey V,Kumar Tiwari R,Ojha RP,Dubey KD
|
|
Journal
|
Molecules (Basel, Switzerland)
|
|
Journal Info
|
2021 Jan 5;26(1):239
|
|
Abstract
|
CD4-mimetic HIV-1 entry inhibitors are small sized molecules which imitate similar conformational flexibility, in gp120, to the CD4 receptor. However, the mechanism of the conformational flexibility instigated by these small sized inhibitors is little known. Likewise, the effect of the antibody on the function of these inhibitors is also less studied. In this study, we present a thorough inspection of the mechanism of the conformational flexibility induced by a CD4-mimetic inhibitor, NBD-557, using Molecular Dynamics Simulations and free energy calculations. Our result shows the functional importance of Asn425 in substrate induced conformational dynamics in gp120. The MD simulations of Asn425Gly mutant provide a less dynamic gp120 in the presence of NBD-557 without incapacitating the binding enthalpy of NBD-557. The MD simulations of complexes with the antibody clearly show the enhanced affinity of NBD-557 due to the presence of the antibody, which is in good agreement with experimental Isothermal Titration Calorimetry results (Biochemistry2006, 45, 10973-10980).
|
|
Sequence Data
|
-
|