Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/141539
Title: Modeling the full length HIV-1 Gag polyprotein reveals the role of its p6 subunit in viral maturation and the effect of non-cleavage site mutations in protease drug resistance
Authors: Su, Chinh Tran-To
Kwoh, Chee-Keong
Verma, Chandra Shekhar
Gan, Samuel Ken-En
Keywords: Engineering::Computer science and engineering
Issue Date: 2017
Source: Su, C. T.-T., Kwoh, C.-K., Verma, C. S., & Gan, S. K.-E. (2018). Modeling the full length HIV-1 Gag polyprotein reveals the role of its p6 subunit in viral maturation and the effect of non-cleavage site mutations in protease drug resistance. Journal of Biomolecular Structure and Dynamics, 36(16), 4366-4377. doi:10.1080/07391102.2017.1417160
Journal: Journal of Biomolecular Structure and Dynamics
Abstract: HIV polyprotein Gag is increasingly found to contribute to protease inhibitor resistance. Despite its role in viral maturation and in developing drug resistance, there remain gaps in the knowledge of the role of certain Gag subunits (e.g. p6), and that of non-cleavage mutations in drug resistance. As p6 is flexible, it poses a problem for structural experiments, and is hence often omitted in experimental Gag structural studies. Nonetheless, as p6 is an indispensable component for viral assembly and maturation, we have modeled the full length Gag structure based on several experimentally determined constraints and studied its structural dynamics. Our findings suggest that p6 can mechanistically modulate Gag conformations. In addition, the full length Gag model reveals that allosteric communication between the non-cleavage site mutations and the first Gag cleavage site could possibly result in protease drug resistance, particularly in the absence of mutations in Gag cleavage sites. Our study provides a mechanistic understanding to the structural dynamics of HIV-1 Gag, and also proposes p6 as a possible drug target in anti-HIV therapy.
URI: https://hdl.handle.net/10356/141539
ISSN: 0739-1102
DOI: 10.1080/07391102.2017.1417160
Rights: © 2017 Informa UK Limited, trading as Taylor & Francis Group. All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SCSE Journal Articles

SCOPUSTM   
Citations

6
checked on Sep 3, 2020

WEB OF SCIENCETM
Citations

7
checked on Oct 26, 2020

Page view(s)

6
checked on Oct 25, 2020

Google ScholarTM

Check

Altmetric


Plumx

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.