Large-scale conformational dynamics of the HIV-1 integrase core domain and its catalytic loop mutants.

ABSTRACT: HIV-1 integrase is one of the three essential enzymes required for viral replication and has great potential as a novel target for anti-HIV drugs. Although tremendous efforts have been devoted to understanding this protein, the conformation of the catalytic core domain around the active site, particularly the catalytic loop overhanging the active site, is still not well characterized by experimental methods due to its high degree of flexibility. Recent studies have suggested that this conformational dynamics is directly correlated with enzymatic activity, but the details of this dynamics is not known. In this study, we conducted a series of extended-time molecular dynamics simulations and locally enhanced sampling simulations of the wild-type and three loop hinge mutants to investigate the

SUBMITTER: Lee MC 

PROVIDER: S-EPMC1305464 | biostudies-literature | 2005 May

REPOSITORIES: biostudies-literature