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The structure of the C-terminal actin-binding domain of talin.

Gingras, Alexandre R, Bate, Neil, Goult, Benjamin T, Hazelwood, Larnele, Canestrelli, Ilona, Grossmann, J Günter, Liu, HongJun, Putz, Nicholas S M, Roberts, Gordon C K, Volkmann, Niels, and others. (2008) The structure of the C-terminal actin-binding domain of talin. The EMBO journal, 27 (2). pp. 458-469. ISSN 1460-2075. (doi:10.1038/sj.emboj.7601965) (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)

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Official URL
http://dx.doi.org/10.1038/sj.emboj.7601965

Abstract

Talin is a large dimeric protein that couples integrins to cytoskeletal actin. Here, we report the structure of the C-terminal actin-binding domain of talin, the core of which is a five-helix bundle linked to a C-terminal helix responsible for dimerisation. The NMR structure of the bundle reveals a conserved surface-exposed hydrophobic patch surrounded by positively charged groups. We have mapped the actin-binding site to this surface and shown that helix 1 on the opposite side of the bundle negatively regulates actin binding. The crystal structure of the dimerisation helix reveals an antiparallel coiled-coil with conserved residues clustered on the solvent-exposed face. Mutagenesis shows that dimerisation is essential for filamentous actin (F-actin) binding and indicates that the dimerisation helix itself contributes to binding. We have used these structures together with small angle X-ray scattering to derive a model of the entire domain. Electron microscopy provides direct evidence for binding of the dimer to F-actin and indicates that it binds to three monomers along the long-pitch helix of the actin filament.

Item Type: Article
DOI/Identification number: 10.1038/sj.emboj.7601965
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Ben Goult
Date Deposited: 07 Aug 2014 15:42 UTC
Last Modified: 13 Aug 2019 03:05 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/42133 (The current URI for this page, for reference purposes)
Goult, Benjamin T: https://orcid.org/0000-0002-3438-2807
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