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{{STRUCTURE_3odo|  PDB=3odo  |  SCENE=  }}
===Crystal Structure of the DH/PH Domains of p115-RhoGEF===


==Function==
==Crystal Structure of the DH/PH Domains of p115-RhoGEF==
[[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>
<StructureSection load='3odo' size='340' side='right'caption='[[3odo]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3odo]] is a 2 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=3ODO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ODO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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=3odo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3odo OCA], [https://pdbe.org/3odo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3odo RCSB], [https://www.ebi.ac.uk/pdbsum/3odo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3odo ProSAT]</span></td></tr>
</table>
== Function ==
[https://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>  


==About this Structure==
==See Also==
[[3odo]] is a 2 chain structure with 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=3ODO OCA].
*[[Rho guanine nucleotide exchange factor 3D structures|Rho guanine nucleotide exchange factor 3D structures]]
 
== References ==
==Reference==
<references/>
<references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Chen, Z.]]
[[Category: Large Structures]]
[[Category: Guo, L.]]
[[Category: Chen Z]]
[[Category: Sprang, S R.]]
[[Category: Guo L]]
[[Category: Sternweis, P C.]]
[[Category: Sprang SR]]
[[Category: Dh]]
[[Category: Sternweis PC]]
[[Category: Ph]]
[[Category: Regulation of rhoa gtpase]]
[[Category: Rho]]
[[Category: Rhogef]]
[[Category: Signaling protein]]

Latest revision as of 12:36, 6 September 2023

Crystal Structure of the DH/PH Domains of p115-RhoGEFCrystal Structure of the DH/PH Domains of p115-RhoGEF

Structural highlights

3odo is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 Also

References

  1. ↑ Hart MJ, Sharma S, elMasry N, Qiu RG, McCabe P, Polakis P, Bollag G. Identification of a novel guanine nucleotide exchange factor for the Rho GTPase. J Biol Chem. 1996 Oct 11;271(41):25452-8. PMID:8810315
  2. ↑ Kozasa T, Jiang X, Hart MJ, Sternweis PM, Singer WD, Gilman AG, Bollag G, Sternweis PC. p115 RhoGEF, a GTPase activating protein for Galpha12 and Galpha13. Science. 1998 Jun 26;280(5372):2109-11. PMID:9641915
  3. ↑ Hart MJ, Jiang X, Kozasa T, Roscoe W, Singer WD, Gilman AG, Sternweis PC, Bollag G. Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13. Science. 1998 Jun 26;280(5372):2112-4. PMID:9641916
  4. ↑ Guilluy C, Bregeon J, Toumaniantz G, Rolli-Derkinderen M, Retailleau K, Loufrani L, Henrion D, Scalbert E, Bril A, Torres RM, Offermanns S, Pacaud P, Loirand G. The Rho exchange factor Arhgef1 mediates the effects of angiotensin II on vascular tone and blood pressure. Nat Med. 2010 Feb;16(2):183-90. doi: 10.1038/nm.2079. Epub 2010 Jan 24. PMID:20098430 doi:10.1038/nm.2079

3odo, resolution 2.90Å

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