Atomic structure of the MAP kinase ERK2 at 2.3 A resolution.
作者： Faming Zhang , Arne Strand , David Robbins , Melanie H. Cobb , Elizabeth J. Goldsmith
DOI: 10.1038/367704A0
关键词:
摘要: The structure of the MAP kinase ERK2, a ubiquitous protein target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to resolution 2.3 A. two domains ERK2 are farther apart than active cAMP-dependent peptide-binding site is blocked tyrosine 185, one residues that phosphorylated enzyme. Activation thus likely involve both global local conformational changes.
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