RNA-induced conformational changes in a viral coat protein studied by hydrogen/deuterium exchange mass spectrometry.

ABSTRACT: A detailed knowledge of the capsid assembly pathways of viruses from their coat protein building blocks is required to devise novel therapeutic strategies to inhibit such assembly. In the quest for understanding how assembly of single-stranded RNA viruses is achieved at the molecular level, HDX-MS has been used to locate regions of a coat protein dimer that exhibit conformational/dynamical changes, and hence changes in their HDX kinetics, upon binding to a genomic RNA stem-loop known to trigger assembly initiation. The HDX-MS data highlight specific areas within the coat protein dimer that alter their exchange kinetics in the presence of the RNA. These include the known RNA-binding sites, β-strands E and G, which have a lower susceptibility to HDX when ligand-bound, as may have been expect

SUBMITTER: Morton VL 

PROVIDER: S-EPMC4782220 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature