Oligomerization of a retroviral matrix protein is facilitated by backbone flexibility on nanosecond time scale.

ABSTRACT: The oligomerization capacity of the retroviral matrix protein is an important feature that affects assembly of immature virions and their interaction with cellular membrane. A combination of NMR relaxation measurements and advanced analysis of molecular dynamics simulation trajectory provided an unprecedentedly detailed insight into internal mobility of matrix proteins of the Mason-Pfizer monkey virus. Strong evidence have been obtained that the oligomerization capacity of the wild-type matrix protein is closely related to the enhanced dynamics of several parts of its backbone on a nanosecond time scale. Increased flexibility has been observed for two regions: the loop between α-helices α2 and α3 and the C-terminal half of α-helix α3 which accommodate amino acid residues that form the olig

SUBMITTER: Srb P 

PROVIDER: S-EPMC3066403 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature