The flexible C-terminal arm of the Lassa arenavirus Z-protein mediates interactions with multiple binding partners.

ABSTRACT: The arenavirus genome encodes for a Z-protein, which contains a RING domain that coordinates two zinc ions, and has been identified as having several functional roles at various stages of the virus life cycle. Z-protein binds to multiple host proteins and has been directly implicated in the promotion of viral budding, repression of mRNA translation, and apoptosis of infected cells. Using homology models of the Z-protein from Lassa strain arenavirus, replica exchange molecular dynamics (MD) was used to refine the structures, which were then subsequently clustered. Population-weighted ensembles of low-energy cluster representatives were predicted based upon optimal agreement of the chemical shifts computed with the SPARTA program with the experimental NMR chemical shifts. A member of the ref

SUBMITTER: May ER 

PROVIDER: S-EPMC2933069 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature