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1p38

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{{STRUCTURE_1p38| PDB=1p38 | SCENE= }}
{{STRUCTURE_1p38| PDB=1p38 | SCENE= }}
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'''THE STRUCTURE OF THE MAP KINASE P38 AT 2.1 ANGSTOMS RESOLUTION'''
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===THE STRUCTURE OF THE MAP KINASE P38 AT 2.1 ANGSTOMS RESOLUTION===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 9122194 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9122194}}
==About this Structure==
==About this Structure==
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[[Category: Serine/threonine-protein kinase]]
[[Category: Serine/threonine-protein kinase]]
[[Category: Transferase]]
[[Category: Transferase]]
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Revision as of 19:56, 28 July 2008

Image:1p38.png

Template:STRUCTURE 1p38

THE STRUCTURE OF THE MAP KINASE P38 AT 2.1 ANGSTOMS RESOLUTION

Template:ABSTRACT PUBMED 9122194

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

Page seeded by OCA on Mon Jul 28 22:56:08 2008

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