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1erk

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Image:1erk.gif

1erk, resolution 2.3Å

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STRUCTURE OF SIGNAL-REGULATED KINASE

Overview

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.

About this Structure

1ERK is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Atomic structure of the MAP kinase ERK2 at 2.3 A resolution., Zhang F, Strand A, Robbins D, Cobb MH, Goldsmith EJ, Nature. 1994 Feb 24;367(6465):704-11. PMID:8107865

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