2p0d

<StructureSection load='2p0d' size='340' side='right' caption='[[2p0d]], [[Resolution|resolution]] 1.81&Aring;' scene=''>

<table><tr><td colspan='2'>[[2p0d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P0D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P0D FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2p0f|2p0f]], [[2p0h|2p0h]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARHGAP9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p0d OCA], [http://pdbe.org/2p0d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p0d RCSB], [http://www.ebi.ac.uk/pdbsum/2p0d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2p0d ProSAT]</span></td></tr>

[[http://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>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p0/2p0d_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2p0d" style="background-color:#fffaf0;"></div>

*[[Rho GTPase activating protein|Rho GTPase activating protein]]

[[Category: Human]]

[[Category: Blasutig, I]]

[[Category: Ceccarelli, D F.J]]

[[Category: Goudreault, M]]

[[Category: Pawson, T]]

[[Category: Ruston, J]]

[[Category: Sicheri, F]]

[[Category: Protein-phosphoinositide complex]]