Impact of M36I polymorphism on the interaction of HIV-1 protease with its substrates: insights from molecular dynamics. - Institut Pasteur Access content directly
Journal Articles BMC Genomics Year : 2014

Impact of M36I polymorphism on the interaction of HIV-1 protease with its substrates: insights from molecular dynamics.

Abstract

Over the last decades, a vast structural knowledge has been gathered on the HIV-1 protease (PR). Noticeably, most of the studies focused the B-subtype, which has the highest prevalence in developed countries. Accordingly, currently available anti-HIV drugs target this subtype, with considerable benefits for the corresponding patients. However, in developing countries, there is a wide variety of HIV-1 subtypes carrying PR polymorphisms related to reduced drug susceptibility. The non-active site mutation, M36I, is the most frequent polymorphism, and is considered as a non-B subtype marker. Yet, the structural impact of this substitution on the PR structure and on the interaction with natural substrates remains poorly documented.
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pasteur-01402879 , version 1 (25-11-2016)

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Mauricio Gs Costa, Técio G Benetti-Barbosa, Nathan Desdouits, Arnaud Blondel, Paulo M Bisch, et al.. Impact of M36I polymorphism on the interaction of HIV-1 protease with its substrates: insights from molecular dynamics.. BMC Genomics, 2014, 15 (Suppl 7), pp.S5. ⟨10.1186/1471-2164-15-S7-S5⟩. ⟨pasteur-01402879⟩

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