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) (KAR id:42133)

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/10.1038/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
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 15:42 UTC
Last Modified:	20 May 2025 09:18 UTC
Resource URI:	https://kar.kent.ac.uk/id/eprint/42133 (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
CReDIT Contributor Roles:

Depositors only (login required):

Altmetric

Total Views

Total unique views of this page since July 2020. For more details click on the image.