2kvp: Difference between revisions

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'''Unreleased structure'''


The entry 2kvp is ON HOLD
==Solution Structure of the R10 Domain of Talin==
<StructureSection load='2kvp' size='340' side='right'caption='[[2kvp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2kvp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KVP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KVP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kvp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kvp OCA], [https://pdbe.org/2kvp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kvp RCSB], [https://www.ebi.ac.uk/pdbsum/2kvp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kvp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TLN1_MOUSE TLN1_MOUSE] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts.
== 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/kv/2kvp_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=2kvp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Talin is a large flexible rod-shaped protein that activates the integrin family of cell adhesion molecules and couples them to cytoskeletal actin. Its rod region consists of a series of helical bundles. Here we show that residues 1815-1973 form a 5-helix bundle, with a topology unique to talin which is optimally suited for formation of a long rod such as talin. This is much more stable than the 4-helix (1843-1973) domain described earlier and as a result its vinculin binding sequence is inaccessible to vinculin at room temperature, with implications for the overall mechanism of the talin-vinculin interaction.


Authors: Goult, B.T., Gingras, A.R., Bate, N., Critchley, D.R., Barsukov, I.L., Roberts, G.C.
The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site.,Goult BT, Gingras AR, Bate N, Barsukov IL, Critchley DR, Roberts GC FEBS Lett. 2010 Jun 3;584(11):2237-41. Epub 2010 Apr 20. PMID:20399778<ref>PMID:20399778</ref>


Description: NMR structure of the talin VBS3 domain, 1815-1973
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kvp" style="background-color:#fffaf0;"></div>


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr  7 10:14:43 2010''
==See Also==
*[[Talin 3D structures|Talin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Barsukov IL]]
[[Category: Bate N]]
[[Category: Critchley DR]]
[[Category: Gingras AR]]
[[Category: Goult BT]]
[[Category: Roberts GC]]