1t01: Difference between revisions

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[[Image:1t01.gif|left|200px]]


{{Structure
==Vinculin complexed with the VBS1 helix from talin==
|PDB= 1t01 |SIZE=350|CAPTION= <scene name='initialview01'>1t01</scene>, resolution 2.06&Aring;
<StructureSection load='1t01' size='340' side='right'caption='[[1t01]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1t01]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T01 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.06&#8491;</td></tr>
|GENE= VCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus]), TLN1, TLN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t01 OCA], [https://pdbe.org/1t01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t01 RCSB], [https://www.ebi.ac.uk/pdbsum/1t01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t01 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/t0/1t01_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=1t01 ConSurf].
<div style="clear:both"></div>


'''Vinculin complexed with the VBS1 helix from talin'''
==See Also==
 
*[[Isocitrate dehydrogenase|Isocitrate dehydrogenase]]
 
*[[Talin 3D structures|Talin 3D structures]]
==Overview==
*[[Vinculin|Vinculin]]
The interaction between the cytoskeletal proteins talin and vinculin plays a key role in integrin-mediated cell adhesion and migration. We have determined the crystal structures of two domains from the talin rod spanning residues 482-789. Talin 482-655, which contains a vinculin-binding site (VBS), folds into a five-helix bundle whereas talin 656-789 is a four-helix bundle. We show that the VBS is composed of a hydrophobic surface spanning five turns of helix 4. All the key side chains from the VBS are buried and contribute to the hydrophobic core of the talin 482-655 fold. We demonstrate that the talin 482-655 five-helix bundle represents an inactive conformation, and mutations that disrupt the hydrophobic core or deletion of helix 5 are required to induce an active conformation in which the VBS is exposed. We also report the crystal structure of the N-terminal vinculin head domain in complex with an activated form of talin. Activation of the VBS in talin and the recruitment of vinculin may support the maturation of small integrin/talin complexes into more stable adhesions.
== References ==
 
<references/>
==About this Structure==
__TOC__
1T01 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T01 OCA].
</StructureSection>
 
==Reference==
Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle., Papagrigoriou E, Gingras AR, Barsukov IL, Bate N, Fillingham IJ, Patel B, Frank R, Ziegler WH, Roberts GC, Critchley DR, Emsley J, EMBO J. 2004 Aug 4;23(15):2942-51. Epub 2004 Jul 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15272303 15272303]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Barsukov IL]]
[[Category: Barsukov, I L.]]
[[Category: Critchley DR]]
[[Category: Critchley, D R.]]
[[Category: Emsley J]]
[[Category: Emsley, J.]]
[[Category: Gingras AR]]
[[Category: Gingras, A R.]]
[[Category: Papagrigoriou E]]
[[Category: Papagrigoriou, E.]]
[[Category: five helix bundle]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:11:51 2008''

Latest revision as of 08:35, 14 February 2024

Vinculin complexed with the VBS1 helix from talin

1t01, resolution 2.06Å

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