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==Crystal Structure of the Linker-DH/PH domains of p115-RhoGEF== | ==Crystal Structure of the Linker-DH/PH domains of p115-RhoGEF== | ||
<StructureSection load='3odw' size='340' side='right' caption='[[3odw]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='3odw' size='340' side='right' caption='[[3odw]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3odo|3odo]], [[1txd|1txd]], [[1xcg|1xcg]], [[3kz1|3kz1]], [[1x86|1x86]], [[3odx|3odx]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3odo|3odo]], [[1txd|1txd]], [[1xcg|1xcg]], [[3kz1|3kz1]], [[1x86|1x86]], [[3odx|3odx]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARHGEF1 ([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">ARHGEF1 ([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=3odw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3odw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3odw RCSB], [http://www.ebi.ac.uk/pdbsum/3odw 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=3odw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3odw OCA], [http://pdbe.org/3odw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3odw RCSB], [http://www.ebi.ac.uk/pdbsum/3odw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3odw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[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> | [[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> | ||
==See Also== | |||
*[[Rho guanine nucleotide exchange factor|Rho guanine nucleotide exchange factor]] | |||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 02:08, 5 August 2016
Crystal Structure of the Linker-DH/PH domains of p115-RhoGEFCrystal Structure of the Linker-DH/PH domains of p115-RhoGEF
Structural highlights
Function[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.[1] [2] [3] [4] See AlsoReferences
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