2p0f: Difference between revisions

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-{{Seed}}
-[[Image:2p0f.png|left|200px]]
-<!--
+==ArhGAP9 PH domain in complex with Ins(1,3,5)P3==
-The line below this paragraph, containing "STRUCTURE_2p0f", creates the "Structure Box" on the page.
+<StructureSection load='2p0f' size='340' side='right'caption='[[2p0f]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
--->
+<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>
-{{STRUCTURE_2p0f|  PDB=2p0f  |  SCENE=  }}
+<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>
+</table>
+== Function ==
+[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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p0/2p0f_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===ArhGAP9 PH domain in complex with Ins(1,3,5)P3===
+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>
+</div>
+<div class="pdbe-citations 2p0f" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17339315}}, adds the Publication Abstract to the page
+*[[Rho GTPase activating protein 3D structures|Rho GTPase activating protein 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17339315 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17339315}}
+__TOC__
+</StructureSection>
-==About this Structure==
-P0F is a 1 chain 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].
-==Reference==
-<ref group="xtra">PMID:17339315</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Blasutig, I.]]
+[[Category: Large Structures]]
-[[Category: Ceccarelli, D F.J.]]
+[[Category: Blasutig I]]
-[[Category: Goudreault, M.]]
+[[Category: Ceccarelli DFJ]]
-[[Category: Pawson, T.]]
+[[Category: Goudreault M]]
-[[Category: Ruston, J.]]
+[[Category: Pawson T]]
-[[Category: Sicheri, F.]]
+[[Category: Ruston J]]
-[[Category: Pleckstrin homology domain]]
+[[Category: Sicheri F]]
-[[Category: Protein-phosphoinositide complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:35:30 2009''