1cc0

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{{Seed}}
 
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[[Image:1cc0.png|left|200px]]
 
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==CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX==
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The line below this paragraph, containing "STRUCTURE_1cc0", creates the "Structure Box" on the page.
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<StructureSection load='1cc0' size='340' side='right'caption='[[1cc0]], [[Resolution|resolution]] 5.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1cc0]] 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=1CC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CC0 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_1cc0| PDB=1cc0 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cc0 OCA], [https://pdbe.org/1cc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cc0 RCSB], [https://www.ebi.ac.uk/pdbsum/1cc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cc0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RHOA_HUMAN RHOA_HUMAN] Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization.<ref>PMID:8910519</ref> <ref>PMID:9121475</ref> <ref>PMID:12900402</ref> <ref>PMID:16103226</ref> <ref>PMID:16236794</ref> <ref>PMID:19934221</ref> <ref>PMID:20937854</ref> <ref>PMID:20974804</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cc/1cc0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1cc0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Like all Rho (Ras homology) GTPases, RhoA functions as a molecular switch in cell signaling, alternating between GTP- and GDP-bound states, with its biologically inactive GDP-bound form maintained as a cytosolic complex with RhoGDI (guanine nucleotide-exchange inhibitor). The crystal structures of RhoA-GDP and of the C-terminal immunoglobulin-like domain of RhoGDI (residues 67-203) are known, but the mechanism by which the two proteins interact is not known. The functional human RhoA-RhoGDI complex has been expressed in yeast and crystallized (P6(5)22, unit-cell parameters a = b = 139, c = 253 A, two complexes in the asymmetric unit). Although diffraction from these crystals extends to 3.5 A and is highly anisotropic, the experimentally phased (MAD plus MIR) electron-density map was adequate to reveal the mutual disposition of the two molecules. The result was validated by molecular-replacement calculations when data were corrected for anisotropy. Furthermore, the N-terminus of RhoGDI (the region involved in inhibition of nucleotide exchange) can be identified in the electron-density map: it is bound to the switch I and switch II regions of RhoA, occluding an epitope which binds Dbl-like nucleotide-exchange factors. The entrance of the hydrophobic pocket of RhoGDI is 25 A from the last residue in the RhoA model, with its C-terminus oriented to accommodate the geranylgeranyl group without conformational change in RhoA.
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===CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX===
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How RhoGDI binds Rho.,Longenecker K, Read P, Derewenda U, Dauter Z, Liu X, Garrard S, Walker L, Somlyo AV, Nakamoto RK, Somlyo AP, Derewenda ZS Acta Crystallogr D Biol Crystallogr. 1999 Sep;55(Pt 9):1503-15. PMID:10489445<ref>PMID:10489445</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1cc0" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10489445}}, adds the Publication Abstract to the page
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*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10489445 is the PubMed ID number.
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*[[Guanine nucleotide dissociation inhibitor|Guanine nucleotide dissociation inhibitor]]
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*[[Rho GTPase 3D structures|Rho GTPase 3D structures]]
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{{ABSTRACT_PUBMED_10489445}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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1CC0 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=1CC0 OCA].
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</StructureSection>
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==Reference==
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How RhoGDI binds Rho., Longenecker K, Read P, Derewenda U, Dauter Z, Liu X, Garrard S, Walker L, Somlyo AV, Nakamoto RK, Somlyo AP, Derewenda ZS, Acta Crystallogr D Biol Crystallogr. 1999 Sep;55(Pt 9):1503-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10489445 10489445]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Dauter, Z.]]
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[[Category: Dauter Z]]
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[[Category: Derewenda, U.]]
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[[Category: Derewenda U]]
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[[Category: Derewenda, Z S.]]
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[[Category: Derewenda ZS]]
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[[Category: Garrard, S.]]
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[[Category: Garrard S]]
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[[Category: Longenecker, K L.]]
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[[Category: Longenecker KL]]
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[[Category: Nakamoto, R K.]]
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[[Category: Nakamoto RK]]
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[[Category: Read, P.]]
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[[Category: Read P]]
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[[Category: Somlyo, A P.]]
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[[Category: Somlyo AP]]
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[[Category: Somlyo, A V.]]
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[[Category: Somlyo AV]]
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[[Category: Walker, L.]]
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[[Category: Walker L]]
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[[Category: G-protein]]
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[[Category: Rho gtpase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:32:03 2008''
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Current revision

CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX

PDB ID 1cc0

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