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1erk

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[[Image:1erk.gif|left|200px]]
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{{STRUCTURE_1erk| PDB=1erk | SCENE= }}
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'''STRUCTURE OF SIGNAL-REGULATED KINASE'''
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===STRUCTURE OF SIGNAL-REGULATED KINASE===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_8107865}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 8107865 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8107865}}
==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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:26:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:45:54 2008''

Revision as of 22:45, 30 June 2008

Template:STRUCTURE 1erk

STRUCTURE OF SIGNAL-REGULATED KINASE

Template:ABSTRACT PUBMED 8107865

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

Page seeded by OCA on Tue Jul 1 01:45:54 2008

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