2j7t

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(New page: 200px<br /> <applet load="2j7t" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j7t, resolution 2.00&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:2j7t.gif|left|200px]]<br />
 
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<applet load="2j7t" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2j7t, resolution 2.00&Aring;" />
 
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'''CRYSTAL STRUCTURE OF HUMAN SERINE THREONINE KINASE-10 BOUND TO SU11274'''<br />
 
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==About this Structure==
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==Crystal structure of human serine threonine kinase-10 bound to SU11274==
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2J7T is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA, ACT and 274 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J7T OCA]].
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<StructureSection load='2j7t' size='340' side='right'caption='[[2j7t]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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[[Category: Homo sapiens]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[2j7t]] 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=2J7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J7T FirstGlance]. <br>
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[[Category: Arrowsmith, C.H.]]
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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&#8491;</td></tr>
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[[Category: Das, S.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=274:(3Z)-N-(3-CHLOROPHENYL)-3-({3,5-DIMETHYL-4-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-1H-PYRROL-2-YL}METHYLENE)-N-METHYL-2-OXOINDOLINE-5-SULFONAMIDE'>274</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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[[Category: Debreczeni, J.]]
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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=2j7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j7t OCA], [https://pdbe.org/2j7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j7t RCSB], [https://www.ebi.ac.uk/pdbsum/2j7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j7t ProSAT]</span></td></tr>
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[[Category: Delft, F.Von.]]
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</table>
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[[Category: Edwards, A.]]
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== Disease ==
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[[Category: Eswaran, J.]]
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[https://www.uniprot.org/uniprot/STK10_HUMAN STK10_HUMAN] The disease may be caused by mutations affecting the gene represented in this entry.<ref>PMID:16175573</ref>
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[[Category: Fedorov, O.]]
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== Function ==
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[[Category: Gorrec, F.]]
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[https://www.uniprot.org/uniprot/STK10_HUMAN STK10_HUMAN] Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo.<ref>PMID:11903060</ref> <ref>PMID:12639966</ref> <ref>PMID:19255442</ref>
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[[Category: Knapp, S.]]
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== Evolutionary Conservation ==
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[[Category: Papagrigoriou, E.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Pike, A.C.W.]]
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Check<jmol>
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[[Category: Rellos, P.]]
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<jmolCheckbox>
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[[Category: Savitsky, P.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j7/2j7t_consurf.spt"</scriptWhenChecked>
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[[Category: Sobott, F.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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[[Category: Sundstrom, M.]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: Turnbull, A.P.]]
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</jmolCheckbox>
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[[Category: Ugochukwa, E.]]
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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=2j7t ConSurf].
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[[Category: Umeano, C.C.]]
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<div style="clear:both"></div>
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[[Category: Watt, S.]]
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<div style="background-color:#fffaf0;">
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[[Category: Weigelt, J.]]
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== Publication Abstract from PubMed ==
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[[Category: 274]]
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Protein kinase autophosphorylation of activation segment residues is a common regulatory mechanism in phosphorylation-dependent signalling cascades. However, the molecular mechanisms that guarantee specific and efficient phosphorylation of these sites have not been elucidated. Here, we report on three novel and diverse protein kinase structures that reveal an exchanged activation segment conformation. This dimeric arrangement results in an active kinase conformation in trans, with activation segment phosphorylation sites in close proximity to the active site of the interacting protomer. Analytical ultracentrifugation and chemical cross-linking confirmed the presence of dimers in solution. Consensus substrate sequences for each kinase showed that the identified activation segment autophosphorylation sites are non-consensus substrate sites. Based on the presented structural and functional data, a model for specific activation segment phosphorylation at non-consensus substrate sites is proposed that is likely to be common to other kinases from diverse subfamilies.
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[[Category: ACT]]
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[[Category: CA]]
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[[Category: atp-binding]]
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[[Category: cell cycle progression]]
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[[Category: coiled coil]]
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[[Category: disease mutation]]
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[[Category: kinase]]
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[[Category: lymphocyte oriented kinase (lok)]]
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[[Category: nucleotide-binding]]
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[[Category: phosphorylation]]
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[[Category: serine/threonine kinase (stk10a)]]
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[[Category: serine/threonine-protein kinase]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:37:27 2007''
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Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites.,Pike AC, Rellos P, Niesen FH, Turnbull A, Oliver AW, Parker SA, Turk BE, Pearl LH, Knapp S EMBO J. 2008 Feb 20;27(4):704-14. Epub 2008 Jan 31. PMID:18239682<ref>PMID:18239682</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 2j7t" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith CH]]
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[[Category: Das S]]
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[[Category: Debreczeni J]]
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[[Category: Edwards A]]
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[[Category: Eswaran J]]
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[[Category: Fedorov O]]
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[[Category: Gorrec F]]
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[[Category: Knapp S]]
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[[Category: Papagrigoriou E]]
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[[Category: Pike ACW]]
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[[Category: Rellos P]]
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[[Category: Savitsky P]]
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[[Category: Sobott F]]
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[[Category: Sundstrom M]]
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[[Category: Turnbull AP]]
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[[Category: Ugochukwa E]]
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[[Category: Umeano CC]]
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[[Category: Watt S]]
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[[Category: Weigelt J]]
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[[Category: Von Delft F]]

Current revision

Crystal structure of human serine threonine kinase-10 bound to SU11274

PDB ID 2j7t

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