Format

Send to

Choose Destination
Nature. 1994 Feb 24;367(6465):704-11.

Atomic structure of the MAP kinase ERK2 at 2.3 A resolution.

Author information

1
Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas.

Abstract

The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes.

PMID:
8107865
DOI:
10.1038/367704a0
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Nature Publishing Group
Loading ...
Support Center