Kinetic characterization of the critical step in HIV-1 protease maturation.

ABSTRACT: HIV maturation requires multiple cleavage of long polyprotein chains into functional proteins that include the viral protease itself. Initial cleavage by the protease dimer occurs from within these precursors, and yet only a single protease monomer is embedded in each polyprotein chain. Self-activation has been proposed to start from a partially dimerized protease formed from monomers of different chains binding its own N termini by self-association to the active site, but a complete structural understanding of this critical step in HIV maturation is missing. Here, we captured the critical self-association of immature HIV-1 protease to its extended amino-terminal recognition motif using large-scale molecular dynamics simulations, thus confirming the postulated intramolecular mechanism in a

SUBMITTER: Sadiq SK 

PROVIDER: S-EPMC3528573 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature