1u6h: Difference between revisions

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New page: left|200px<br /><applet load="1u6h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u6h, resolution 2.38Å" /> '''Vinculin head (0-258...
 
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[[Image:1u6h.gif|left|200px]]<br /><applet load="1u6h" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1u6h, resolution 2.38&Aring;" />
'''Vinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)'''<br />


==Overview==
==Vinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)==
The cytoskeletal protein talin plays a key role in activating integrins, and in coupling them to the actin cytoskeleton. Its N-terminal globular, head, which binds beta integrins, is linked to an extended rod having a, C-terminal actin binding site and several vinculin binding sites (VBSs)., The NMR structure of residues 755-889 of the rod (containing a VBS) is, shown to be an amphipathic four-helix bundle with a left-handed topology., A talin peptide corresponding to the VBS binds the vinculin head; the, X-ray crystallographic structure of this complex shows that the residues, which interact with vinculin are buried in the hydrophobic core of the, talin fragment. NMR shows that the interaction involves a major structural, change in the talin fragment, including unfolding of one of its helices, making the VBS accessible to vinculin. Interestingly, the talin 755-889, fragment binds more than one vinculin head molecule, suggesting that the, talin rod may contain additional as yet unrecognized VBSs.
<StructureSection load='1u6h' size='340' side='right'caption='[[1u6h]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1u6h]] 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=1U6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U6H FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u6h OCA], [https://pdbe.org/1u6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u6h RCSB], [https://www.ebi.ac.uk/pdbsum/1u6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u6h ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u6/1u6h_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1u6h ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1U6H is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U6H OCA].
*[[Talin 3D structures|Talin 3D structures]]
 
*[[Vinculin 3D structures|Vinculin 3D structures]]
==Reference==
== References ==
A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head., Fillingham I, Gingras AR, Papagrigoriou E, Patel B, Emsley J, Critchley DR, Roberts GC, Barsukov IL, Structure. 2005 Jan;13(1):65-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15642262 15642262]
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Barsukov, I.L.]]
[[Category: Barsukov IL]]
[[Category: Critchley, D.R.]]
[[Category: Critchley DR]]
[[Category: Emsley, J.]]
[[Category: Emsley J]]
[[Category: Fillingham, I.]]
[[Category: Fillingham I]]
[[Category: Gingras, A.R.]]
[[Category: Gingras AR]]
[[Category: Papagrigoriou, E.]]
[[Category: Papagrigoriou E]]
[[Category: Patel, B.]]
[[Category: Patel B]]
[[Category: Roberts, G.C.K.]]
[[Category: Roberts GCK]]
[[Category: protein-protein complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:52:43 2007''

Latest revision as of 09:16, 3 April 2024

Vinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)Vinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)

Structural highlights

1u6h is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.38Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Zhang Z, Izaguirre G, Lin SY, Lee HY, Schaefer E, Haimovich B. The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading. Mol Biol Cell. 2004 Sep;15(9):4234-47. Epub 2004 Jun 30. PMID:15229287 doi:10.1091/mbc.E04-03-0264
  2. ↑ le Duc Q, Shi Q, Blonk I, Sonnenberg A, Wang N, Leckband D, de Rooij J. Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner. J Cell Biol. 2010 Jun 28;189(7):1107-15. doi: 10.1083/jcb.201001149. PMID:20584916 doi:10.1083/jcb.201001149
  3. ↑ Peng X, Cuff LE, Lawton CD, DeMali KA. Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin. J Cell Sci. 2010 Feb 15;123(Pt 4):567-77. doi: 10.1242/jcs.056432. Epub 2010 Jan , 19. PMID:20086044 doi:10.1242/jcs.056432

1u6h, resolution 2.38Å

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