1xwj

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[[Image:1xwj.gif|left|200px]]
 
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{{Structure
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==Vinculin head (1-258) in complex with the talin vinculin binding site 3 (1945-1969)==
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|PDB= 1xwj |SIZE=350|CAPTION= <scene name='initialview01'>1xwj</scene>, resolution 2.60&Aring;
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<StructureSection load='1xwj' size='340' side='right'caption='[[1xwj]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1xwj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XWJ FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.6&#8491;</td></tr>
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|GENE=
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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=1xwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xwj OCA], [https://pdbe.org/1xwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xwj RCSB], [https://www.ebi.ac.uk/pdbsum/1xwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xwj ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xwj OCA], [http://www.ebi.ac.uk/pdbsum/1xwj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xwj RCSB]</span>
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[https://www.uniprot.org/uniprot/VINC_CHICK VINC_CHICK] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:15229287</ref> <ref>PMID:20584916</ref> <ref>PMID:20086044</ref>
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}}
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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/xw/1xwj_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=1xwj ConSurf].
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<div style="clear:both"></div>
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'''Vinculin head (1-258) in complex with the talin vinculin binding site 3 (1945-1969)'''
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==See Also==
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*[[Talin 3D structures|Talin 3D structures]]
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*[[Vinculin|Vinculin]]
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==Overview==
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== References ==
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Talin is a key protein involved in linking integrins to the actin cytoskeleton. The long flexible talin rod domain contains a number of binding sites for vinculin, a cytoskeletal protein important in stabilizing integrin-mediated cell-matrix junctions. Here we report the solution structure of a talin rod polypeptide (residues 1843-1973) which contains a single vinculin binding site (VBS; residues 1944-1969). Like other talin rod polypeptides, it consists of a helical bundle, in this case a four-helix bundle with a right-handed topology. The residues in the VBS important for vinculin binding were identified by studying the binding of a series of VBS-related peptides to the vinculin Vd1 domain. The key binding determinants are buried in the interior of the helical bundle, suggesting that a substantial structural change in the talin polypeptide is required for vinculin binding. Direct evidence for this was obtained by NMR and EPR spectroscopy. [1H,15N]-HSQC spectra of the talin fragment indicate that vinculin binding caused approximately two-thirds of the protein to adopt a flexible random coil. For EPR spectroscopy, nitroxide spin labels were attached to the talin polypeptide via appropriately located cysteine residues. Measurements of inter-nitroxide distances in doubly spin-labeled protein showed clearly that the helical bundle is disrupted and the mobility of the helices, except for the VBS helix, is markedly increased. Binding of vinculin to talin is thus a clear example of the unusual phenomenon of protein unfolding being required for protein/protein interaction.
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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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1XWJ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XWJ OCA].
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==Reference==
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Structural and dynamic characterization of a vinculin binding site in the talin rod., Gingras AR, Vogel KP, Steinhoff HJ, Ziegler WH, Patel B, Emsley J, Critchley DR, Roberts GC, Barsukov IL, Biochemistry. 2006 Feb 14;45(6):1805-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16460027 16460027]
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Barsukov, I L.]]
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[[Category: Barsukov IL]]
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[[Category: Critchley, D R.]]
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[[Category: Critchley DR]]
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[[Category: Emsley, J.]]
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[[Category: Emsley J]]
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[[Category: Gingras, A R.]]
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[[Category: Gingras AR]]
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[[Category: Papagrigoriou, E.]]
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[[Category: Papagrigoriou E]]
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[[Category: talin]]
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[[Category: vinculin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:55:38 2008''
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Current revision

Vinculin head (1-258) in complex with the talin vinculin binding site 3 (1945-1969)

PDB ID 1xwj

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