2p0f

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[[Image:2p0f.jpg|left|200px]]
 
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{{Structure
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==ArhGAP9 PH domain in complex with Ins(1,3,5)P3==
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|PDB= 2p0f |SIZE=350|CAPTION= <scene name='initialview01'>2p0f</scene>, resolution 1.91&Aring;
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<StructureSection load='2p0f' size='340' side='right'caption='[[2p0f]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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<table><tr><td colspan='2'>[[2p0f]] 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=2P0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P0F 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]] 1.91&#8491;</td></tr>
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|GENE= ARHGAP9 ([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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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}}
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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=2p0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p0f OCA], [https://pdbe.org/2p0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p0f RCSB], [https://www.ebi.ac.uk/pdbsum/2p0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p0f ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RHG09_HUMAN RHG09_HUMAN] GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has a substantial GAP activity toward CDC42 and RAC1 and less toward RHOA. Has a role in regulating adhesion of hematopoietic cells to the extracellular matrix.<ref>PMID:11396949</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/p0/2p0f_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=2p0f 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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Pleckstrin homology (PH) domains are phosphoinositide (PI)-binding modules that target proteins to membrane surfaces. Here we define a family of PH domain proteins, including Tiam1 and ArhGAP9, that demonstrates specificity for PI(4,5)P(2), as well as for PI(3,4,5)P(3) and PI(3,4)P(2), the products of PI 3-kinase. These PH domain family members utilize a non-canonical phosphoinositide binding pocket related to that employed by beta-spectrin. Crystal structures of the PH domain of ArhGAP9 in complex with the headgroups of Ins(1,3,4)P(3), Ins(1,4,5)P(3), and Ins(1,3,5)P(3) reveal how two adjacent phosphate positions in PI(3,4)P(2), PI(4,5)P(2), and PI(3,4,5)P(3) are accommodated through flipped conformations of the bound phospholipid. We validate the non-canonical site of phosphoinositide interaction by showing that binding pocket mutations, which disrupt phosphoinositide binding in vitro, also disrupt membrane localization of Tiam1 in cells. We posit that the diversity in PI interaction modes displayed by PH domains contributes to their versatility of use in biological systems.
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'''ArhGAP9 PH domain in complex with Ins(1,3,5)P3'''
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Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9.,Ceccarelli DF, Blasutig IM, Goudreault M, Li Z, Ruston J, Pawson T, Sicheri F J Biol Chem. 2007 May 4;282(18):13864-74. Epub 2007 Mar 5. PMID:17339315<ref>PMID:17339315</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 2p0f" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Pleckstrin homology (PH) domains are phosphoinositide (PI)-binding modules that target proteins to membrane surfaces. Here we define a family of PH domain proteins, including Tiam1 and ArhGAP9, that demonstrates specificity for PI(4,5)P(2), as well as for PI(3,4,5)P(3) and PI(3,4)P(2), the products of PI 3-kinase. These PH domain family members utilize a non-canonical phosphoinositide binding pocket related to that employed by beta-spectrin. Crystal structures of the PH domain of ArhGAP9 in complex with the headgroups of Ins(1,3,4)P(3), Ins(1,4,5)P(3), and Ins(1,3,5)P(3) reveal how two adjacent phosphate positions in PI(3,4)P(2), PI(4,5)P(2), and PI(3,4,5)P(3) are accommodated through flipped conformations of the bound phospholipid. We validate the non-canonical site of phosphoinositide interaction by showing that binding pocket mutations, which disrupt phosphoinositide binding in vitro, also disrupt membrane localization of Tiam1 in cells. We posit that the diversity in PI interaction modes displayed by PH domains contributes to their versatility of use in biological systems.
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*[[Rho GTPase activating protein 3D structures|Rho GTPase activating protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2P0F 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=2P0F OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9., Ceccarelli DF, Blasutig IM, Goudreault M, Li Z, Ruston J, Pawson T, Sicheri F, J Biol Chem. 2007 May 4;282(18):13864-74. Epub 2007 Mar 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17339315 17339315]
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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: Blasutig, I.]]
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[[Category: Blasutig I]]
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[[Category: Ceccarelli, D F.J.]]
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[[Category: Ceccarelli DFJ]]
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[[Category: Goudreault, M.]]
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[[Category: Goudreault M]]
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[[Category: Pawson, T.]]
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[[Category: Pawson T]]
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[[Category: Ruston, J.]]
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[[Category: Ruston J]]
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[[Category: Sicheri, F.]]
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[[Category: Sicheri F]]
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[[Category: PO4]]
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[[Category: pleckstrin homology domain]]
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[[Category: protein-phosphoinositide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:06:56 2008''
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Current revision

ArhGAP9 PH domain in complex with Ins(1,3,5)P3

PDB ID 2p0f

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