2QDQ
Crystal structure of the talin dimerisation domain
Summary for 2QDQ
Entry DOI | 10.2210/pdb2qdq/pdb |
Descriptor | Talin-1 (2 entities in total) |
Functional Keywords | talin, dimerisation domain, c-terminal actin binding site, abs3, latch domain, structural protein |
Biological source | Mus musculus (house mouse) |
Cellular location | Cell projection, ruffle membrane ; Peripheral membrane protein ; Cytoplasmic side : P26039 |
Total number of polymer chains | 2 |
Total formula weight | 11695.45 |
Authors | Gingras, A.R.,Putz, N.S.M.,Bate, N.,Barsukov, I.L.,Critchley, D.R.C. (deposition date: 2007-06-21, release date: 2008-01-29, Last modification date: 2024-02-21) |
Primary citation | Gingras, A.R.,Bate, N.,Goult, B.T.,Hazelwood, L.,Canestrelli, I.,Grossmann, J.G.,Liu, H.,Putz, N.S.,Roberts, G.C.,Volkmann, N.,Hanein, D.,Barsukov, I.L.,Critchley, D.R. The structure of the C-terminal actin-binding domain of talin. Embo J., 27:458-469, 2008 Cited by PubMed 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. PubMed: 18157087DOI: 10.1038/sj.emboj.7601965 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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