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2oud

From Proteopedia

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[[Image:2oud.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of the catalytic domain of human MKP5==
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|PDB= 2oud |SIZE=350|CAPTION= <scene name='initialview01'>2oud</scene>, resolution 2.80&Aring;
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<StructureSection load='2oud' size='340' side='right'caption='[[2oud]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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<table><tr><td colspan='2'>[[2oud]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OUD FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.8&#8491;</td></tr>
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|GENE= MKP5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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|DOMAIN=
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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=2oud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oud OCA], [https://pdbe.org/2oud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oud RCSB], [https://www.ebi.ac.uk/pdbsum/2oud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oud ProSAT]</span></td></tr>
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|RELATEDENTRY=[[2ouc|2OUC]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oud OCA], [http://www.ebi.ac.uk/pdbsum/2oud PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oud RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/DUS10_HUMAN DUS10_HUMAN] Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily.<ref>PMID:22375048</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/ou/2oud_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=2oud ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of the catalytic domain of human MKP5'''
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==See Also==
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*[[MAP kinase phosphatase|MAP kinase phosphatase]]
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== References ==
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==Overview==
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<references/>
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MAP kinase phosphatases (MKPs) have crucial roles in regulating the signaling activity of MAP kinases and are potential targets for drug discovery against human diseases. These enzymes contain a catalytic domain (CD) as well as a binding domain (BD) that help recognize the target MAP kinase. We report here the crystal structures at up to 2.2 A resolution of the BD and CD of human MKP5 and compare them to the known structures from other MKPs. Dramatic structural differences are observed between the BD of MKP5 and that of MKP3 determined previously by NMR. In particular, the cluster of positively charged residues that is important for MAP kinase binding is located in completely different positions in the two structures, with a distance of 25 A between them. Moreover, this cluster is alpha-helical in MKP5, while it forms a loop followed by a beta-strand in MKP3. These large structural differences could be associated with the distinct substrate preferences of these phosphatases, but further studies are needed to confirm this. The CD of MKP5 is observed in an active conformation, and two loops in the active site have backbone shifts of up to 5 A relative to the inactive CDs from other MKPs.
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__TOC__
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</StructureSection>
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==About this Structure==
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2OUD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OUD OCA].
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==Reference==
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Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5., Tao X, Tong L, Protein Sci. 2007 May;16(5):880-6. Epub 2007 Mar 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17400920 17400920]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Tao, X.]]
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[[Category: Tao X]]
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[[Category: Tong, L.]]
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[[Category: Tong L]]
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[[Category: a central five-stranded b-sheet]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:23:15 2008''
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Current revision

Crystal structure of the catalytic domain of human MKP5

PDB ID 2oud

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