The Structure of Mitogen-activated Protein Kinase P38 at 2.1-A Resolution

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1997 Mar 18

PMID 9122194

Citations 84

Authors

Z Wang

P C Harkins

R J Ulevitch

J Han

M H Cobb

E J Goldsmith

Affiliations

Soon will be listed here.

Abstract

The structure of mitogen-activated protein (MAP) kinase p38 has been solved at 2.1-A to an R factor of 21.0%, making p38 the second low activity MAP kinase solved to date. Although p38 is topologically similar to the MAP kinase ERK2, the phosphorylation Lip (a regulatory loop near the active site) adopts a different fold in p38. The peptide substrate binding site and the ATP binding site are also different from those of ERK2. The results explain why MAP kinases are specific for different activating enzymes, substrates, and inhibitors. A model presented for substrate and activator interactions has implications for the evolution of protein kinase cascades.

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