The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site.

Goult, Benjamin T, Gingras, Alexandre R, Bate, Neil, Barsukov, Igor L, Critchley, David R, Roberts, Gordon C K (2010) The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site. FEBS letters, 584 (11). pp. 2237-2241. ISSN 1873-3468. (doi:10.1016/j.febslet.2010.04.028) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:42125)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL: http://dx.doi.org/10.1016/j.febslet.2010.04.028

Abstract

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.

Item Type:	Article
DOI/Identification number:	10.1016/j.febslet.2010.04.028
Subjects:	Q Science > QH Natural history > QH301 Biology
Institutional Unit:	Schools > School of Natural Sciences > Biosciences
Former Institutional Unit:	Divisions > Division of Natural Sciences > Biosciences
Depositing User:	Ben Goult
Date Deposited:	07 Aug 2014 15:53 UTC
Last Modified:	20 May 2025 09:18 UTC
Resource URI:	https://kar.kent.ac.uk/id/eprint/42125 (The current URI for this page, for reference purposes)

University of Kent Author Information

Goult, Benjamin T.

Creator's ORCID:	https://orcid.org/0000-0002-3438-2807
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