2erk

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{{STRUCTURE_2erk| PDB=2erk | SCENE= }}
{{STRUCTURE_2erk| PDB=2erk | SCENE= }}
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'''PHOSPHORYLATED MAP KINASE ERK2'''
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===PHOSPHORYLATED MAP KINASE ERK2===
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==Overview==
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The structure of the active form of the MAP kinase ERK2 has been solved, phosphorylated on a threonine and a tyrosine residue within the phosphorylation lip. The lip is refolded, bringing the phosphothreonine and phosphotyrosine into alignment with surface arginine-rich binding sites. Conformational changes occur in the lip and neighboring structures, including the P+1 site, the MAP kinase insertion, the C-terminal extension, and helix C. Domain rotation and remodeling of the proline-directed P+1 specificity pocket account for the activation. The conformation of the P+1 pocket is similar to a second proline-directed kinase, CDK2-CyclinA, thus permitting the origin of this specificity to be defined. Conformational changes outside the lip provide loci at which the state of phosphorylation can be felt by other cellular components.
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(as it appears on PubMed at http://www.pubmed.gov), where 9298898 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9298898}}
==About this Structure==
==About this Structure==
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[[Category: Phosphotransferase]]
[[Category: Phosphotransferase]]
[[Category: Serine/threonine-protein kinase]]
[[Category: Serine/threonine-protein kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:38:10 2008''

Revision as of 21:38, 28 July 2008

Image:2erk.png

Template:STRUCTURE 2erk

PHOSPHORYLATED MAP KINASE ERK2

Template:ABSTRACT PUBMED 9298898

About this Structure

2ERK is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation., Canagarajah BJ, Khokhlatchev A, Cobb MH, Goldsmith EJ, Cell. 1997 Sep 5;90(5):859-69. PMID:9298898

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