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

Mauricio Gs Costa (1, 2) , Técio G Benetti-Barbosa (1) , Nathan Desdouits (3) , Arnaud Blondel (3) , Paulo M Bisch (1) , Pedro G Pascutti (1) , Paulo R Batista (3, 2, 1)

1 IBCCF / UFRJ - Instituto de Biofísica Carlos Chagas Filho [Rio de Janeiro]
2 PROCC - Program for Scientific Computing / Programa de Computação Científica [Rio de Janeiro]
3 Bioinformatique structurale - Structural Bioinformatics

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.

Domaines: Bio-Informatique, Biologie Systémique [q-bio.QM]

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⟩