Biophysical analysis of the MHR motif in folding and domain swapping of the HIV capsid protein C-terminal domain.

ABSTRACT: Infection by human immunodeficiency virus (HIV) depends on the function, in virion morphogenesis and other stages of the viral cycle, of a highly conserved structural element, the major homology region (MHR), within the carboxyterminal domain (CTD) of the capsid protein. In a modified CTD dimer, MHR is swapped between monomers. While no evidence for MHR swapping has been provided by structural models of retroviral capsids, it is unknown whether it may occur transiently along the virus assembly pathway. Whatever the case, the MHR-swapped dimer does provide a novel target for the development of anti-HIV drugs based on the concept of trapping a nonnative capsid protein conformation. We have carried out a thermodynamic and kinetic characterization of the domain-swapped CTD dimer in solution. T

SUBMITTER: Bocanegra R 

PROVIDER: S-EPMC4302195 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature