Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/141539
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dc.contributor.authorSu, Chinh Tran-Toen_US
dc.contributor.authorKwoh, Chee-Keongen_US
dc.contributor.authorVerma, Chandra Shekharen_US
dc.contributor.authorGan, Samuel Ken-Enen_US
dc.date.accessioned2020-06-09T03:33:54Z-
dc.date.available2020-06-09T03:33:54Z-
dc.date.issued2017-
dc.identifier.citationSu, 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:10.1080/07391102.2017.1417160en_US
dc.identifier.issn0739-1102en_US
dc.identifier.urihttps://hdl.handle.net/10356/141539-
dc.description.abstractHIV 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.en_US
dc.description.sponsorshipASTAR (Agency for Sci., Tech. and Research, S’pore)en_US
dc.language.isoenen_US
dc.relation.ispartofJournal of Biomolecular Structure and Dynamicsen_US
dc.rights© 2017 Informa UK Limited, trading as Taylor & Francis Group. All rights reserved.en_US
dc.subjectEngineering::Computer science and engineeringen_US
dc.titleModeling 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 resistanceen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Computer Science and Engineeringen_US
dc.identifier.doi10.1080/07391102.2017.1417160-
dc.identifier.pmid29237328-
dc.identifier.scopus2-s2.0-85039153566-
dc.identifier.issue16en_US
dc.identifier.volume36en_US
dc.identifier.spage4366en_US
dc.identifier.epage4377en_US
dc.subject.keywordsFull Length HIV-1 Gag Structureen_US
dc.subject.keywordsP6 Subuniten_US
item.fulltextNo Fulltext-
item.grantfulltextnone-
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