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2v55

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{{Seed}}
 
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[[Image:2v55.png|left|200px]]
 
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==Mechanism of multi-site phosphorylation from a ROCK-I:RhoE complex structure==
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The line below this paragraph, containing "STRUCTURE_2v55", creates the "Structure Box" on the page.
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<StructureSection load='2v55' size='340' side='right'caption='[[2v55]], [[Resolution|resolution]] 3.71&Aring;' scene=''>
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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'>[[2v55]] 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=2V55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V55 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]] 3.705&#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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2v55| PDB=2v55 | 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=2v55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v55 OCA], [https://pdbe.org/2v55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v55 RCSB], [https://www.ebi.ac.uk/pdbsum/2v55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v55 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ROCK1_HUMAN ROCK1_HUMAN] 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 DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles. Promotes keratinocyte terminal differentiation.<ref>PMID:8617235</ref> <ref>PMID:9722579</ref> <ref>PMID:10436159</ref> <ref>PMID:10652353</ref> <ref>PMID:11018042</ref> <ref>PMID:11283607</ref> <ref>PMID:17158456</ref> <ref>PMID:18694941</ref> <ref>PMID:18573880</ref> <ref>PMID:19036714</ref> <ref>PMID:19181962</ref> <ref>PMID:19131646</ref> <ref>PMID:19997641</ref> <ref>PMID:21072057</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/v5/2v55_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=2v55 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 ROCK-I serine/threonine protein kinase mediates the effects of RhoA to promote the formation of actin stress fibres and integrin-based focal adhesions. ROCK-I phosphorylates the unconventional G-protein RhoE on multiple N- and C-terminal sites. These phosphorylation events stabilise RhoE, which functions to antagonise RhoA-induced stress fibre assembly. Here, we provide a molecular explanation for multi-site phosphorylation of RhoE from the crystal structure of RhoE in complex with the ROCK-I kinase domain. RhoE interacts with the C-lobe alphaG helix of ROCK-I by means of a novel binding site remote from its effector region, positioning its N and C termini proximal to the ROCK-I catalytic site. Disruption of the ROCK-I:RhoE interface abolishes RhoE phosphorylation, but has no effect on the ability of RhoE to disassemble stress fibres. In contrast, mutation of the RhoE effector region attenuates RhoE-mediated disruption of the actin cytoskeleton, indicating that RhoE exerts its inhibitory effects on ROCK-I through protein(s) binding to its effector region. We propose that ROCK-I phosphorylation of RhoE forms part of a feedback loop to regulate RhoA signalling.
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===MECHANISM OF MULTI-SITE PHOSPHORYLATION FROM A ROCK-I:RHOE COMPLEX STRUCTURE===
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Mechanism of multi-site phosphorylation from a ROCK-I:RhoE complex structure.,Komander D, Garg R, Wan PT, Ridley AJ, Barford D EMBO J. 2008 Dec 3;27(23):3175-85. Epub 2008 Oct 23. PMID:18946488<ref>PMID:18946488</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 2v55" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18946488}}, 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 18946488 is the PubMed ID number.
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*[[Rho GTPase 3D structures|Rho GTPase 3D structures]]
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*[[Rho-associated protein kinase 3D structures|Rho-associated protein kinase 3D structures]]
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{{ABSTRACT_PUBMED_18946488}}
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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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2V55 is a 4 chains 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=2V55 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:18946488</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Large Structures]]
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[[Category: Barford, D.]]
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[[Category: Barford D]]
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[[Category: Garg, R.]]
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[[Category: Garg R]]
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[[Category: Komander, D.]]
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[[Category: Komander D]]
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[[Category: Ridley, A J.]]
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[[Category: Ridley AJ]]
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[[Category: Wan, P T.C.]]
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[[Category: Wan PTC]]
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[[Category: Apoptosis]]
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[[Category: Atp-binding]]
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[[Category: Coiled coil]]
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[[Category: Cytoplasm]]
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[[Category: G-protein]]
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[[Category: Golgi apparatus]]
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[[Category: Gtp-binding]]
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[[Category: Kinase]]
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[[Category: Lipoprotein]]
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[[Category: Membrane]]
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[[Category: Metal-binding]]
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[[Category: Methylation]]
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[[Category: Multi-site phosphorylation]]
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[[Category: Nucleotide-binding]]
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[[Category: Phorbol-ester binding]]
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[[Category: Phosphoprotein]]
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[[Category: Polymorphism]]
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[[Category: Prenylation]]
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[[Category: Rhoe]]
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[[Category: Rock-i]]
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[[Category: Serine/threonine-protein kinase]]
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[[Category: Stress fibre]]
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[[Category: Transferase]]
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[[Category: Zinc]]
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[[Category: Zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 23:56:06 2009''
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Current revision

Mechanism of multi-site phosphorylation from a ROCK-I:RhoE complex structure

PDB ID 2v55

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