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| | <StructureSection load='2p0h' size='340' side='right'caption='[[2p0h]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2p0h' size='340' side='right'caption='[[2p0h]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2p0h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P0H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2p0h]] 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=2P0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P0H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I3S:(1S,3S,4S)-1,3,4-TRIPHOSPHO-MYO-INOSITOL'>I3S</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2p0d|2p0d]], [[2p0f|2p0f]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I3S:(1S,3S,4S)-1,3,4-TRIPHOSPHO-MYO-INOSITOL'>I3S</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARHGAP9 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2p0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p0h OCA], [https://pdbe.org/2p0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p0h RCSB], [https://www.ebi.ac.uk/pdbsum/2p0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p0h ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p0h OCA], [https://pdbe.org/2p0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p0h RCSB], [https://www.ebi.ac.uk/pdbsum/2p0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p0h ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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>
| + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blasutig, I]] | + | [[Category: Blasutig I]] |
| - | [[Category: Ceccarelli, D F.J]] | + | [[Category: Ceccarelli DFJ]] |
| - | [[Category: Goudreault, M]] | + | [[Category: Goudreault M]] |
| - | [[Category: Pawson, T]] | + | [[Category: Pawson T]] |
| - | [[Category: Ruston, J]] | + | [[Category: Ruston J]] |
| - | [[Category: Sicheri, F]] | + | [[Category: Sicheri F]] |
| - | [[Category: Ligand binding protein]]
| + | |
| - | [[Category: Pleckstrin homology domain]]
| + | |
| - | [[Category: Protein-phosphoinositide complex]]
| + | |
| Structural highlights
Function
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.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Furukawa Y, Kawasoe T, Daigo Y, Nishiwaki T, Ishiguro H, Takahashi M, Kitayama J, Nakamura Y. Isolation of a novel human gene, ARHGAP9, encoding a rho-GTPase activating protein. Biochem Biophys Res Commun. 2001 Jun 15;284(3):643-9. PMID:11396949 doi:http://dx.doi.org/10.1006/bbrc.2001.5022
- ↑ Ceccarelli DF, Blasutig IM, Goudreault M, Li Z, Ruston J, Pawson T, Sicheri F. Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9. J Biol Chem. 2007 May 4;282(18):13864-74. Epub 2007 Mar 5. PMID:17339315 doi:http://dx.doi.org/10.1074/jbc.M700505200
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