Distinct patterns of activation-dependent changes in conformational mobility between ERK1 and ERK2.

ABSTRACT: Hydrogen/deuterium exchange measurements by mass spectrometry (HX-MS) can be used to report localized conformational mobility within folded proteins, where exchange predominantly occurs through low energy fluctuations in structure, allowing transient solvent exposure. Changes in conformational mobility may impact protein function, even in cases where structural changes are unobservable. Previous studies of the MAP kinase, ERK2, revealed increases in HX upon activation occured at the hinge between conserved N- and C-terminal domains, which could be ascribed to enhanced backbone flexibility. This implied that kinase activation modulates interdomain closure, and was supported by evidence for two modes of nucleotide binding that were consistent with closed vs open conformations in active vs in

SUBMITTER: Ring AY 

PROVIDER: S-EPMC3139246 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature