Interdomain salt-bridges in the Ebola virus protein VP40 and their role in domain association and plasma membrane localization.

ABSTRACT: The Ebola virus protein VP40 is a transformer protein that possesses an extraordinary ability to accomplish multiple functions by transforming into various oligomeric conformations. The disengagement of the C-terminal domain (CTD) from the N-terminal domain (NTD) is a crucial step in the conformational transformations of VP40 from the dimeric form to the hexameric form or octameric ring structure. Here, we use various molecular dynamics (MD) simulations to investigate the dynamics of the VP40 protein and the roles of interdomain interactions that are important for the domain-domain association and dissociation, and report on experimental results of the behavior of mutant variants of VP40. The MD studies find that various salt-bridge interactions modulate the VP40 domain dynamics by providi

SUBMITTER: Gc JB 

PROVIDER: S-EPMC5338242 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature