2JSW
Solution Structure of the R13 Domain of Talin
Summary for 2JSW
| Entry DOI | 10.2210/pdb2jsw/pdb |
| Related | 2QDQ |
| NMR Information | BMRB: 15411 |
| Descriptor | Talin-1 (1 entity in total) |
| Functional Keywords | talin, c-terminal actin binding site, abs3, thatch domain, cytoskeleton, phosphorylation, structural protein, actin-binding protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P26039 |
| Total number of polymer chains | 1 |
| Total formula weight | 19379.87 |
| Authors | Goult, B.T.,Gingras, A.R.,Bate, N.,Critchley, D.R.C.,Barsukov, I.L. (deposition date: 2007-07-17, release date: 2008-01-29, Last modification date: 2024-05-29) |
| 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, 2007 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 | SOLUTION NMR |
Structure validation
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