2jsw
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NMR structure of the talin C-terminal actin binding site
OverviewOverview
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.
About this StructureAbout this Structure
2JSW is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
The structure of the C-terminal actin-binding domain of talin., 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, EMBO J. 2008 Jan 23;27(2):458-69. Epub 2007 Dec 20. PMID:18157087
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