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1uix

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(New page: 200px<br /><applet load="1uix" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uix, resolution 1.8&Aring;" /> '''Coiled-coil structure...)
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[[Image:1uix.jpg|left|200px]]<br /><applet load="1uix" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1uix, resolution 1.8&Aring;" />
 
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'''Coiled-coil structure of the RhoA-binding domain in Rho-kinase'''<br />
 
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==Overview==
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==Coiled-coil structure of the RhoA-binding domain in Rho-kinase==
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Rho-kinase is a serine/threonine protein kinase that regulates, cytoskeletal events in cells. The enzyme activity of Rho-kinase is, auto-inhibited in the free state but is activated through direct binding, to the small GTPase Rho in the GTP-bound form. The crystal structure of, the Rho-binding domain (RhoBD) of Rho-kinase has been determined at 1.8-A, resolution by the multi-wavelength anomalous dispersion technique. The, structure shows that RhoBD dimerizes to form a parallel coiled-coil with, long consecutive alpha-helices extended to approximately 97 A and suggests, that free Rho-kinase can also form a dimer through parallel, self-association. At the middle region of the coiled-coil, the polypeptide, chains are flexible and display loose "knobs-into-holes" packing of the, side chains from both chains. RhoBD residues that have been shown to be, critical for Rho-binding are spread in the positively charged C-terminal, region. The parallel coiled-coil structure of our Rho-kinase RhoBD in the, free form is different from the anti-parallel coiled-coil structure of, RhoBD of protein kinase N when complexed with RhoA. Implications derived, from these structural studies in relation to the mechanism of Rho-kinase, activation will be addressed with previously reported experimental data.
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<StructureSection load='1uix' size='340' side='right'caption='[[1uix]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1uix]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UIX 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]] 1.8&#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=MSE:SELENOMETHIONINE'>MSE</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=1uix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uix OCA], [https://pdbe.org/1uix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uix RCSB], [https://www.ebi.ac.uk/pdbsum/1uix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uix ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ROCK2_BOVIN ROCK2_BOVIN] Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus.<ref>PMID:8641286</ref> <ref>PMID:8702756</ref> <ref>PMID:9565595</ref> <ref>PMID:9456324</ref> <ref>PMID:10209029</ref> <ref>PMID:10873572</ref> <ref>PMID:10818093</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/ui/1uix_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1uix 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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Rho-kinase is a serine/threonine protein kinase that regulates cytoskeletal events in cells. The enzyme activity of Rho-kinase is auto-inhibited in the free state but is activated through direct binding to the small GTPase Rho in the GTP-bound form. The crystal structure of the Rho-binding domain (RhoBD) of Rho-kinase has been determined at 1.8-A resolution by the multi-wavelength anomalous dispersion technique. The structure shows that RhoBD dimerizes to form a parallel coiled-coil with long consecutive alpha-helices extended to approximately 97 A and suggests that free Rho-kinase can also form a dimer through parallel self-association. At the middle region of the coiled-coil, the polypeptide chains are flexible and display loose "knobs-into-holes" packing of the side chains from both chains. RhoBD residues that have been shown to be critical for Rho-binding are spread in the positively charged C-terminal region. The parallel coiled-coil structure of our Rho-kinase RhoBD in the free form is different from the anti-parallel coiled-coil structure of RhoBD of protein kinase N when complexed with RhoA. Implications derived from these structural studies in relation to the mechanism of Rho-kinase activation will be addressed with previously reported experimental data.
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==About this Structure==
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Parallel coiled-coil association of the RhoA-binding domain in Rho-kinase.,Shimizu T, Ihara K, Maesaki R, Amano M, Kaibuchi K, Hakoshima T J Biol Chem. 2003 Nov 14;278(46):46046-51. Epub 2003 Sep 3. PMID:12954645<ref>PMID:12954645</ref>
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1UIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UIX 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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Parallel coiled-coil association of the RhoA-binding domain in Rho-kinase., Shimizu T, Ihara K, Maesaki R, Amano M, Kaibuchi K, Hakoshima T, J Biol Chem. 2003 Nov 14;278(46):46046-51. Epub 2003 Sep 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12954645 12954645]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1uix" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Amano, M.]]
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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: Maesaki, R.]]
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[[Category: Shimizu, T.]]
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[[Category: coiled-coil]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:10:03 2007''
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==See Also==
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*[[Rho-associated protein kinase 3D structures|Rho-associated protein kinase 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: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Amano M]]
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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: Maesaki R]]
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[[Category: Shimizu T]]

Current revision

Coiled-coil structure of the RhoA-binding domain in Rho-kinase

PDB ID 1uix

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