View source for 2lqg


==Solution Structure of the R4 domain of talin==
<StructureSection load='2lqg' size='340' side='right'caption='[[2lqg]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lqg]] 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=2LQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQG 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=2lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lqg OCA], [https://pdbe.org/2lqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lqg RCSB], [https://www.ebi.ac.uk/pdbsum/2lqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lqg 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Talin activates integrins, couples them to F-actin and recruits vinculin to focal adhesions (FAs). Here we report the structural characterization of the talin rod, 13 helical bundles (R1-R13) organized into a compact cluster of 4-helix bundles (R2-R4) within a linear chain of 5-helix bundles. Nine of the bundles contain vinculin-binding sites (VBSs) - R2R3 are atypical each containing two VBSs. Talin R2R3 also binds synergistically to RIAM, a Rap1 effector involved in integrin activation. Biochemical and structural data show that vinculin and RIAM binding to R2R3 is mutually exclusive. Moreover, vinculin binding requires domain unfolding while RIAM binds the folded R2R3 double domain. In cells, RIAM is enriched in nascent adhesions at the leading edge whereas vinculin is enriched in FAs, and expression of the talin-binding domain of vinculin displaces RIAM from FAs. We propose a model in which RIAM binding to R2R3 initially recruits talin to membranes where it activates integrins. As talin engages F-actin, force exerted on R2R3 disrupts RIAM binding and exposes the VBSs, which recruit vinculin to stabilize the complex.

RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover.,Goult BT, Zacharchenko T, Bate N, Tsang R, Hey F, Gingras AR, Elliott PR, Roberts GC, Ballestrem C, Critchley DR, Barsukov IL J Biol Chem. 2013 Feb 6. PMID:23389036<ref>PMID:23389036</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lqg" style="background-color:#fffaf0;"></div>

==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 GCK]]