2gph

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[[Image:2gph.gif|left|200px]]<br /><applet load="2gph" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2gph.gif|left|200px]]
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caption="2gph, resolution 1.900&Aring;" />
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'''Docking motif interactions in the MAP kinase ERK2'''<br />
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{{Structure
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|PDB= 2gph |SIZE=350|CAPTION= <scene name='initialview01'>2gph</scene>, resolution 1.900&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Mitogen-activated_protein_kinase Mitogen-activated protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.24 2.7.11.24]
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|GENE= Erk2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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}}
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'''Docking motif interactions in the MAP kinase ERK2'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2GPH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Mitogen-activated_protein_kinase Mitogen-activated protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.24 2.7.11.24] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GPH OCA].
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2GPH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GPH OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16765894 16765894]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16765894 16765894]
[[Category: Mitogen-activated protein kinase]]
[[Category: Mitogen-activated protein kinase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: processing conformation]]
[[Category: processing conformation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:34:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:07:25 2008''

Revision as of 15:07, 20 March 2008


PDB ID 2gph

Drag the structure with the mouse to rotate
, resolution 1.900Å
Gene: Erk2 (Rattus norvegicus)
Activity: Mitogen-activated protein kinase, with EC number 2.7.11.24
Coordinates: save as pdb, mmCIF, xml



Docking motif interactions in the MAP kinase ERK2


Overview

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.

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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