2KVP
Solution Structure of the R10 Domain of Talin
Summary for 2KVP
| Entry DOI | 10.2210/pdb2kvp/pdb |
| Descriptor | Talin-1 (1 entity in total) |
| Functional Keywords | vbs, vinculin, talin, helical bundle, cytoplasm, cytoskeleton, membrane, phosphoprotein, structural protein, acetylation, cell membrane, cell projection |
| Biological source | Mus musculus (mouse) |
| Cellular location | Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P26039 |
| Total number of polymer chains | 1 |
| Total formula weight | 17281.36 |
| Authors | Goult, B.T.,Gingras, A.R.,Bate, N.,Critchley, D.R.,Barsukov, I.L.,Roberts, G.C. (deposition date: 2010-03-24, release date: 2010-05-05, Last modification date: 2024-05-22) |
| Primary citation | Goult, B.T.,Gingras, A.R.,Bate, N.,Barsukov, I.L.,Critchley, D.R.,Roberts, G.C. The domain structure of talin: Residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site. Febs Lett., 584:2237-2241, 2010 Cited by PubMed Abstract: Talin is a large flexible rod-shaped protein that activates the integrin family of cell adhesion molecules and couples them to cytoskeletal actin. Its rod region consists of a series of helical bundles. Here we show that residues 1815-1973 form a 5-helix bundle, with a topology unique to talin which is optimally suited for formation of a long rod such as talin. This is much more stable than the 4-helix (1843-1973) domain described earlier and as a result its vinculin binding sequence is inaccessible to vinculin at room temperature, with implications for the overall mechanism of the talin-vinculin interaction. PubMed: 20399778DOI: 10.1016/j.febslet.2010.04.028 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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