2gph

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[[Image:2gph.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_2gph| PDB=2gph | SCENE= }}
{{STRUCTURE_2gph| PDB=2gph | SCENE= }}
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'''Docking motif interactions in the MAP kinase ERK2'''
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===Docking motif interactions in the MAP kinase ERK2===
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==Overview==
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MAP kinases bind activating kinases, phosphatases, and substrates through docking interactions. Here, we report a 1.9 A crystallographic analysis of inactive ERK2 bound to a "D motif" docking peptide (pepHePTP) derived from hematopoietic tyrosine phosphatase, a negative regulator of ERK2. In this complex, the complete D motif interaction defined by mutagenic analysis is observed, including extensive electrostatic interactions with the "CD" site of the kinase. Large conformational changes occur in the activation loop where the dual phosphorylation sites, which are buried in the inactive form of ERK2, become exposed to solvent in the complex. Similar conformational changes occur in a complex between ERK2 and a MEK2 (MAP/ERK kinase-2)-derived D motif peptide (pepMEK2). D motif peptides are known to bind homologous loci in the MAP kinases p38alpha and JNK1, also inducing conformational changes in these enzymes. However, the binding interactions and conformational changes are unique to each, thus contributing to specificity among MAP kinases.
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The line below this paragraph, {{ABSTRACT_PUBMED_16765894}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16765894 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16765894}}
==About this Structure==
==About this Structure==
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[[Category: Phosphatase-derived peptide]]
[[Category: Phosphatase-derived peptide]]
[[Category: Processing conformation]]
[[Category: Processing conformation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:22:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:54:58 2008''

Revision as of 15:55, 27 July 2008

Template:STRUCTURE 2gph

Docking motif interactions in the MAP kinase ERK2

Template:ABSTRACT PUBMED 16765894

About this Structure

2GPH is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Docking interactions induce exposure of activation loop in the MAP kinase ERK2., Zhou T, Sun L, Humphreys J, Goldsmith EJ, Structure. 2006 Jun;14(6):1011-9. PMID:16765894

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