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2gph

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[[Image:2gph.gif|left|200px]]
 
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{{Structure
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==Docking motif interactions in the MAP kinase ERK2==
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|PDB= 2gph |SIZE=350|CAPTION= <scene name='initialview01'>2gph</scene>, resolution 1.900&Aring;
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<StructureSection load='2gph' size='340' side='right'caption='[[2gph]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2gph]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GPH FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gph OCA], [https://pdbe.org/2gph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gph RCSB], [https://www.ebi.ac.uk/pdbsum/2gph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gph ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PTN7_HUMAN PTN7_HUMAN] Protein phosphatase that acts preferentially on tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T and B-lymphocyte development and signal transduction.<ref>PMID:1510684</ref> <ref>PMID:1530918</ref> <ref>PMID:9624114</ref> <ref>PMID:10206983</ref> <ref>PMID:10559944</ref> <ref>PMID:10702794</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/2gph_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gph ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''Docking motif interactions in the MAP kinase ERK2'''
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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:16765894<ref>PMID:16765894</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2gph" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Mitogen-activated protein kinase 3D structures|Mitogen-activated protein kinase 3D structures]]
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*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
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==About this Structure==
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== References ==
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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].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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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]
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[[Category: Homo sapiens]]
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[[Category: Mitogen-activated protein kinase]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Goldsmith, E J.]]
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[[Category: Goldsmith EJ]]
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[[Category: Humphreys, J.]]
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[[Category: Humphreys J]]
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[[Category: Sun, L.]]
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[[Category: Sun L]]
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[[Category: Zhou, T.]]
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[[Category: Zhou T]]
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[[Category: allostery]]
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[[Category: cd-site]]
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[[Category: d-motif]]
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[[Category: docking interaction]]
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[[Category: erk2]]
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[[Category: phosphatase-derived peptide]]
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[[Category: processing conformation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:07:25 2008''
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Current revision

Docking motif interactions in the MAP kinase ERK2

PDB ID 2gph

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