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1p38

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Image:1p38.gif

1p38, resolution 2.1Å

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THE STRUCTURE OF THE MAP KINASE P38 AT 2.1 ANGSTOMS RESOLUTION

Overview

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.

About this Structure

1P38 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The structure of mitogen-activated protein kinase p38 at 2.1-A resolution., Wang Z, Harkins PC, Ulevitch RJ, Han J, Cobb MH, Goldsmith EJ, Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2327-32. PMID:9122194

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