1u5g

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[[Image:1u5g.gif|left|200px]]<br /><applet load="1u5g" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1u5g, resolution 2.1&Aring;" />
 
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'''Crystal Structure of the PH Domain of SKAP-Hom'''<br />
 
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==About this Structure==
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==Crystal Structure of the PH Domain of SKAP-Hom==
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1U5G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1U5G OCA].
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<StructureSection load='1u5g' size='340' side='right'caption='[[1u5g]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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[[Category: Mus musculus]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[1u5g]] is a 4 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=1U5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U5G FirstGlance]. <br>
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[[Category: Eck, M J.]]
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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]] 2.1&#8491;</td></tr>
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[[Category: Neel, B G.]]
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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=1u5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u5g OCA], [https://pdbe.org/1u5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u5g RCSB], [https://www.ebi.ac.uk/pdbsum/1u5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u5g ProSAT]</span></td></tr>
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[[Category: Swanson, K.]]
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</table>
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[[Category: Tang, Y.]]
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== Function ==
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[[Category: ph domain]]
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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/u5/1u5g_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=1u5g 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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:45 2008''
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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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<div class="pdbe-citations 1u5g" style="background-color:#fffaf0;"></div>
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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: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Eck MJ]]
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[[Category: Neel BG]]
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[[Category: Swanson K]]
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[[Category: Tang Y]]

Current revision

Crystal Structure of the PH Domain of SKAP-Hom

PDB ID 1u5g

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