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[[Image:1xcg.gif|left|200px]]


{{Structure
==Crystal Structure of Human RhoA in complex with DH/PH fragment of PDZRHOGEF==
|PDB= 1xcg |SIZE=350|CAPTION= <scene name='initialview01'>1xcg</scene>, resolution 2.50&Aring;
<StructureSection load='1xcg' size='340' side='right'caption='[[1xcg]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1xcg]] is a 4 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=1XCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XCG FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|GENE= ARHGEF11, KIAA0380 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RHOA, ARHA, ARH12, RHO12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xcg OCA], [https://pdbe.org/1xcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xcg RCSB], [https://www.ebi.ac.uk/pdbsum/1xcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xcg ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARHGB_HUMAN ARHGB_HUMAN] May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xc/1xcg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xcg ConSurf].
<div style="clear:both"></div>


'''Crystal Structure of Human RhoA in complex with DH/PH fragment of PDZRHOGEF'''
==See Also==
 
*[[Rho GTPase 3D structures|Rho GTPase 3D structures]]
 
*[[Rho guanine nucleotide exchange factor 3D structures|Rho guanine nucleotide exchange factor 3D structures]]
==Overview==
__TOC__
Calcium sensitization in smooth muscle is mediated by the RhoA GTPase, activated by hitherto unspecified nucleotide exchange factors (GEFs) acting downstream of Galphaq/Galpha(12/13) trimeric G proteins. Here, we show that at least one potential GEF, the PDZRhoGEF, is present in smooth muscle, and its isolated DH/PH fragment induces calcium sensitization in the absence of agonist-mediated signaling. In vitro, the fragment shows high selectivity for the RhoA GTPase. Full-length fragment is required for the nucleotide exchange, as the isolated DH domain enhances it only marginally. We crystallized the DH/PH fragment of PDZRhoGEF in complex with nonprenylated human RhoA and determined the structure at 2.5 A resolution. The refined molecular model reveals that the mutual disposition of the DH and PH domains is significantly different from other previously described complexes involving DH/PH tandems, and that the PH domain interacts with RhoA in a unique mode. The DH domain makes several specific interactions with RhoA residues not conserved among other Rho family members, suggesting the molecular basis for the observed specificity.
</StructureSection>
 
==About this Structure==
1XCG is a [[Protein complex]] structure of sequences 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=1XCG OCA].
 
==Reference==
The crystal structure of RhoA in complex with the DH/PH fragment of PDZRhoGEF, an activator of the Ca(2+) sensitization pathway in smooth muscle., Derewenda U, Oleksy A, Stevenson AS, Korczynska J, Dauter Z, Somlyo AP, Otlewski J, Somlyo AV, Derewenda ZS, Structure. 2004 Nov;12(11):1955-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15530360 15530360]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Dauter, Z.]]
[[Category: Dauter Z]]
[[Category: Derewenda, U.]]
[[Category: Derewenda U]]
[[Category: Derewenda, Z S.]]
[[Category: Derewenda ZS]]
[[Category: Korczynska, J.]]
[[Category: Korczynska J]]
[[Category: Oleksy, A.]]
[[Category: Oleksy A]]
[[Category: Otlewski, J.]]
[[Category: Otlewski J]]
[[Category: Somlyo, A P.]]
[[Category: Somlyo AP]]
[[Category: Somlyo, A V.]]
[[Category: Somlyo AV]]
[[Category: Stevenson, A S.]]
[[Category: Stevenson AS]]
[[Category: x-ray crystallography; regulation of rhoa gtpase; protein complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:07:55 2008''
Retrieved from "https://proteopedia.org/1xcg"