View source for 6fq4


==Structure of Chlamydial virulence factor TarP and vinculin head domain==
<StructureSection load='6fq4' size='340' side='right' caption='[[6fq4]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fq4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FQ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FQ4 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fq4 OCA], [http://pdbe.org/6fq4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fq4 RCSB], [http://www.ebi.ac.uk/pdbsum/6fq4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fq4 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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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== Publication Abstract from PubMed ==
Vinculin is a central component of mechanosensitive adhesive complexes that form between cells and the extracellular matrix. A myriad of infectious agents mimic vinculin binding sites (VBS), enabling them to hijack the adhesion machinery and facilitate cellular entry. Here, we report the structural and biochemical characterisation of a VBS from the chlamydial virulence factor TarP. Whilst the affinities of isolated VBS peptides from TarP and talin for vinculin are similar, their behaviour in larger fragments is markedly different. In talin, VBS are cryptic and require mechanical activation to bind vinculin, whereas the TarP VBS are located in disordered regions, and so are constitutively active. We demonstrate that the TarP VBS can uncouple talin:vinculin complexes, which may lead to adhesion destabilisation. This article is protected by copyright. All rights reserved.

Chlamydial virulence factor TarP mimics talin to disrupt the talin-vinculin complex.,Whitewood A, Singh AK, Brown DG, Goult BT FEBS Lett. 2018 Apr 30. doi: 10.1002/1873-3468.13074. PMID:29710402<ref>PMID:29710402</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6fq4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Brown, D G]]
[[Category: Goult, B T]]
[[Category: Singh, A K]]
[[Category: Whitewood, A J]]
[[Category: Cell adhesion]]
[[Category: Protein complex]]
[[Category: Translocated actin recruitment protein]]
[[Category: Vinculin-binding site]]
[[Category: Virulence factor]]