2p0h

From Proteopedia

(Difference between revisions)

Revision as of 13:10, 9 June 2021

ArhGAP9 PH domain in complex with Ins(1,3,4)P3

Structural highlights

2p0h is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2p0d, 2p0f
Gene:	ARHGAP9 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2p0h"

@@ Line 1: / Line 1: @@
 ==ArhGAP9 PH domain in complex with Ins(1,3,4)P3==
-<StructureSection load='2p0h' size='340' side='right' caption='[[2p0h]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='2p0h' size='340' side='right'caption='[[2p0h]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2p0h]] 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=2P0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/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/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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=I3S:(1S,3S,4S)-1,3,4-TRIPHOSPHO-MYO-INOSITOL'>I3S</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2p0d|2p0d]], [[2p0f|2p0f]]</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='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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p0h OCA], [http://pdbe.org/2p0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p0h RCSB], [http://www.ebi.ac.uk/pdbsum/2p0h PDBsum], [http://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>
 == Function ==
-[[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>
+[[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]]
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[Rho GTPase activating protein|Rho GTPase activating protein]]
+*[[Rho GTPase activating protein 3D structures|Rho GTPase activating protein 3D structures]]
 == References ==
 <references/>
@@ Line 38: / Line 38: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Blasutig, I]]
 [[Category: Ceccarelli, D F.J]]

2p0h

From Proteopedia

Revision as of 13:10, 9 June 2021

ArhGAP9 PH domain in complex with Ins(1,3,4)P3

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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