Stabilization of the β-hairpin in Mason-Pfizer monkey virus capsid protein- a critical step for infectivity.

ABSTRACT:

Background

Formation of a mature core is a crucial event for infectivity of retroviruses such as Mason-Pfizer monkey virus (M-PMV). The process is triggered by proteolytic cleavage of the polyprotein precursor Gag, which releases matrix, capsid (CA), and nucleocapsid proteins. Once released, CA assembles to form a mature core - a hexameric lattice protein shell that protects retroviral genomic RNA. Subtle conformational changes within CA induce the transition from the immature lattice to the mature lattice. Upon release from the precursor, the initially unstructured N-terminus of CA is refolded to form a β-hairpin stabilized by a salt bridge between the N-terminal proline and conserved aspartate. Although the crucial role of the β-hairpin in the mature core assembly has been confir

SUBMITTER: Obr M 

PROVIDER: S-EPMC4219007 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature