2otx

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{{Seed}}
 
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[[Image:2otx.png|left|200px]]
 
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==Crystal Structure of A N-terminal Fragment of SKAP-HOM Containing both the Helical Dimerization Domain and the PH Domain==
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The line below this paragraph, containing "STRUCTURE_2otx", creates the "Structure Box" on the page.
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<StructureSection load='2otx' size='340' side='right'caption='[[2otx]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2otx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OTX FirstGlance]. <br>
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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]] 2.6&#8491;</td></tr>
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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=2otx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2otx OCA], [https://pdbe.org/2otx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2otx RCSB], [https://www.ebi.ac.uk/pdbsum/2otx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2otx ProSAT]</span></td></tr>
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{{STRUCTURE_2otx| PDB=2otx | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SKAP2_MOUSE SKAP2_MOUSE] May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway.<ref>PMID:11063873</ref> <ref>PMID:15894167</ref> <ref>PMID:16135797</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/ot/2otx_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=2otx 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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PH domains, by binding to phosphoinositides, often serve as membrane-targeting modules. Using crystallographic, biochemical, and cell biological approaches, we have uncovered a mechanism that the integrin-signaling adaptor Skap-hom uses to mediate cytoskeletal interactions. Skap-hom is a homodimer containing an N-terminal four-helix bundle dimerization domain, against which its two PH domains pack in a conformation incompatible with phosphoinositide binding. The isolated PH domains bind PI[3,4,5]P(3), and mutations targeting the dimerization domain or the PH domain's PI[3,4,5]P(3)-binding pocket prevent Skap-hom localization to ruffles. Targeting is retained when the PH domain is deleted or by combined mutation of the PI[3,4,5]P(3)-binding pocket and the PH/dimerization domain interface. Thus, the dimerization and PH domain form a PI[3,4,5]P(3)-responsive molecular switch that controls Skap-hom function.
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===Crystal Structure of A N-terminal Fragment of SKAP-HOM Containing both the Helical Dimerization Domain and the PH Domain===
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The Skap-hom dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch.,Swanson KD, Tang Y, Ceccarelli DF, Poy F, Sliwa JP, Neel BG, Eck MJ Mol Cell. 2008 Nov 21;32(4):564-75. PMID:19026786<ref>PMID:19026786</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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The line below this paragraph, {{ABSTRACT_PUBMED_19026786}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2otx" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19026786 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19026786}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2OTX is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OTX OCA].
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==Reference==
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<ref group="xtra">PMID:19026786</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Eck, M J.]]
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[[Category: Eck MJ]]
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[[Category: Neel, B G.]]
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[[Category: Neel BG]]
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[[Category: Swanson, K D.]]
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[[Category: Swanson KD]]
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[[Category: Tang, Y.]]
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[[Category: Tang Y]]
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[[Category: Novel dimerization domain]]
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[[Category: Ph domain]]
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[[Category: Signaling protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jan 18 09:59:03 2010''
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Current revision

Crystal Structure of A N-terminal Fragment of SKAP-HOM Containing both the Helical Dimerization Domain and the PH Domain

PDB ID 2otx

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