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

ABSTRACT:

Background

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.

Results

Herein, we used molecular dynamics simulations to investigate the role of this polymorphism on the interaction of PR with six of its natural cleavage-sites substrates.

Conclusions

With multiple approaches and analyses we identified structural and dynamical determinants associated with the changes found in the binding affinity of the M36I variant. This mutation influences the flexibility of both PR and its complexed sub

SUBMITTER: Costa MG 

PROVIDER: S-EPMC4243740 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature