Phosphorylation-dependent changes in structure and dynamics in ERK2 detected by SDSL and EPR.

ABSTRACT: Mitogen-activated protein kinases are regulated by occupancy at two phosphorylation sites near the active site cleft. Previous studies using hydrogen exchange to investigate the canonical mitogen-activated protein kinase, extracellular signal-regulated protein kinase-2, have shown that phosphorylation alters backbone conformational mobility >10 A distal to the site of phosphorylation, including decreased mobility within amino acids 102-105 and increased mobility within 108-109. To further describe changes after enzyme activation, site-directed spin labeling at amino acids 101, 105-109, 111, 112 and electron paramagnetic resonance spectroscopy were used to investigate this region. The anisotropic hyperfine splitting of the spin labels in glassy samples was unchanged by phosphorylation, cons

SUBMITTER: Hoofnagle AN 

PROVIDER: S-EPMC1303804 | biostudies-literature | 2004 Jan

REPOSITORIES: biostudies-literature