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Title: The structure of the C-terminal actin-binding domain of talin.
Authors: Gingras, AR
Bate, N
Goult, BT
Hazelwood, L
Canestrelli, I
Grossmann, JG
Liu, H
Putz, NS
Roberts, GC
Volkmann, N
Hanein, D
Barsukov, IL
Critchley, DR
First Published: 23-Jan-2008
Citation: EMBO J, 2008, 27 (2), pp. 458-469
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.
DOI Link: 10.1038/sj.emboj.7601965
eISSN: 1460-2075
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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