2k2r

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{{Seed}}
 
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[[Image:2k2r.png|left|200px]]
 
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==The NMR structure of alpha-parvin CH2/paxillin LD1 complex==
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The line below this paragraph, containing "STRUCTURE_2k2r", creates the "Structure Box" on the page.
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<StructureSection load='2k2r' size='340' side='right'caption='[[2k2r]]' 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'>[[2k2r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K2R 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">Solution NMR</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=2k2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2r OCA], [https://pdbe.org/2k2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k2r RCSB], [https://www.ebi.ac.uk/pdbsum/2k2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2r ProSAT]</span></td></tr>
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{{STRUCTURE_2k2r| PDB=2k2r | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PARVA_HUMAN PARVA_HUMAN] Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration.<ref>PMID:11331308</ref> <ref>PMID:11134073</ref> <ref>PMID:15284246</ref> <ref>PMID:20393563</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/k2/2k2r_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=2k2r 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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Alpha-parvin is an essential component of focal adhesions (FAs), which are large multiprotein complexes that link the plasma membrane and actin cytoskeleton. Alpha-parvin contains two calponin homology (CH) domains and its C-terminal CH2 domain binds multiple targets including paxillin LD motifs for regulating the FA network and signaling. Here we describe the solution structure of alpha-parvin CH2 bound to paxillin LD1. We show that although CH2 contains the canonical CH-fold, a previously defined N-terminal linker forms an alpha-helix that packs unexpectedly with the C-terminal helix of CH2, resulting in a novel variant of the CH domain. Importantly, such packing generates a hydrophobic surface that recognizes the Leu-rich face of paxillin-LD1, and the binding pattern differs drastically from the classical paxillin-LD binding to four-helix bundle proteins such as focal adhesion kinase. These results define a novel modular recognition mode and reveal how alpha-parvin associates with paxillin to mediate the FA assembly and signaling.
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===The NMR structure of alpha-parvin CH2/paxillin LD1 complex===
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The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly.,Wang X, Fukuda K, Byeon IJ, Velyvis A, Wu C, Gronenborn A, Qin J J Biol Chem. 2008 Jul 25;283(30):21113-9. Epub 2008 May 28. PMID:18508764<ref>PMID:18508764</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 2k2r" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18508764}}, adds the Publication Abstract to the page
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*[[Parvin 3D structures|Parvin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18508764 is the PubMed ID number.
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*[[Paxillin|Paxillin]]
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== References ==
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{{ABSTRACT_PUBMED_18508764}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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2K2R is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K2R OCA].
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==Reference==
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<ref group="xtra">PMID:18508764</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Byeon, I.]]
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[[Category: Large Structures]]
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[[Category: Fukuda, K.]]
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[[Category: Byeon I]]
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[[Category: Gronenborn, A.]]
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[[Category: Fukuda K]]
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[[Category: Qin, J.]]
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[[Category: Gronenborn A]]
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[[Category: Velyvis, A.]]
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[[Category: Qin J]]
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[[Category: Wang, X.]]
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[[Category: Velyvis A]]
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[[Category: Wu, C.]]
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[[Category: Wang X]]
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[[Category: Actin-binding]]
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[[Category: Wu C]]
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[[Category: Alternative splicing]]
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[[Category: Cell adhesion]]
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[[Category: Cell junction]]
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[[Category: Cytoplasm]]
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[[Category: Cytoskeleton]]
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[[Category: Lim domain]]
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[[Category: Metal-binding]]
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[[Category: Phosphoprotein]]
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[[Category: Protein complex]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 06:54:06 2009''
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Current revision

The NMR structure of alpha-parvin CH2/paxillin LD1 complex

PDB ID 2k2r

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