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1cxz

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(New page: 200px<br /> <applet load="1cxz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cxz, resolution 2.2&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1cxz.gif|left|200px]]<br />
 
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<applet load="1cxz" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cxz, resolution 2.2&Aring;" />
 
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'''CRYSTAL STRUCTURE OF HUMAN RHOA COMPLEXED WITH THE EFFECTOR DOMAIN OF THE PROTEIN KINASE PKN/PRK1'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF HUMAN RHOA COMPLEXED WITH THE EFFECTOR DOMAIN OF THE PROTEIN KINASE PKN/PRK1==
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The small G protein Rho has emerged as a key regulator of cellular events, involving cytoskeletal reorganization. Here we report the 2.2 A crystal, structure of RhoA bound to an effector domain of protein kinase PKN/PRK1., The structure reveals the antiparallel coiled-coil finger (ACC finger), fold of the effector domain that binds to the Rho specificity-determining, regions containing switch I, beta strands B2 and B3, and the C-terminal, alpha helix A5, predominantly by specific hydrogen bonds. The ACC finger, fold is distinct from those for other small G proteins and provides, evidence for the diverse ways of effector recognition. Sequence analysis, based on the structure suggests that the ACC finger fold is widespread in, Rho effector proteins.
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<StructureSection load='1cxz' size='340' side='right'caption='[[1cxz]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cxz]] 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=1CXZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CXZ FirstGlance]. <br>
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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]] 2.2&#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=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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=1cxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cxz OCA], [https://pdbe.org/1cxz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cxz RCSB], [https://www.ebi.ac.uk/pdbsum/1cxz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cxz 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/cx/1cxz_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=1cxz 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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The small G protein Rho has emerged as a key regulator of cellular events involving cytoskeletal reorganization. Here we report the 2.2 A crystal structure of RhoA bound to an effector domain of protein kinase PKN/PRK1. The structure reveals the antiparallel coiled-coil finger (ACC finger) fold of the effector domain that binds to the Rho specificity-determining regions containing switch I, beta strands B2 and B3, and the C-terminal alpha helix A5, predominantly by specific hydrogen bonds. The ACC finger fold is distinct from those for other small G proteins and provides evidence for the diverse ways of effector recognition. Sequence analysis based on the structure suggests that the ACC finger fold is widespread in Rho effector proteins.
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==About this Structure==
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The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1.,Maesaki R, Ihara K, Shimizu T, Kuroda S, Kaibuchi K, Hakoshima T Mol Cell. 1999 Nov;4(5):793-803. PMID:10619026<ref>PMID:10619026</ref>
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1CXZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and GSP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CXZ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1., Maesaki R, Ihara K, Shimizu T, Kuroda S, Kaibuchi K, Hakoshima T, Mol Cell. 1999 Nov;4(5):793-803. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10619026 10619026]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1cxz" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Hakoshima, T.]]
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[[Category: Ihara, K.]]
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[[Category: Kaibuchi, K.]]
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[[Category: Kuroda, S.]]
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[[Category: Maesaki, R.]]
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[[Category: Shimizu, T.]]
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[[Category: GSP]]
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[[Category: MG]]
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[[Category: antiparallel coiled-coil]]
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[[Category: protein-protein complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:26:36 2007''
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==See Also==
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*[[Rho GTPase 3D structures|Rho GTPase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Hakoshima T]]
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[[Category: Ihara K]]
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[[Category: Kaibuchi K]]
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[[Category: Kuroda S]]
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[[Category: Maesaki R]]
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[[Category: Shimizu T]]

Current revision

CRYSTAL STRUCTURE OF HUMAN RHOA COMPLEXED WITH THE EFFECTOR DOMAIN OF THE PROTEIN KINASE PKN/PRK1

PDB ID 1cxz

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