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3p6a

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<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=3p6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p6a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p6a RCSB], [http://www.ebi.ac.uk/pdbsum/3p6a PDBsum]</span></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=3p6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p6a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p6a RCSB], [http://www.ebi.ac.uk/pdbsum/3p6a PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/ARHG1_HUMAN ARHG1_HUMAN]] Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12. Mediates angiotensin-2-induced RhoA activation.<ref>PMID:8810315</ref> <ref>PMID:9641915</ref> <ref>PMID:9641916</ref> <ref>PMID:20098430</ref>
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== References ==
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<references/>
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__TOC__
</StructureSection>
</StructureSection>

Revision as of 10:00, 25 December 2014

Crystal Structure of the DH/PH domains of p115-RhoGEF (R399E mutant)

3p6a, resolution 2.50Å

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