| First Author | Goult BT | Year | 2010 |
| Journal | FEBS Lett | Volume | 584 |
| Issue | 11 | Pages | 2237-41 |
| PubMed ID | 20399778 | Mgi Jnum | J:160366 |
| Mgi Id | MGI:4454350 | Doi | 10.1016/j.febslet.2010.04.028 |
| Citation | Goult BT, et al. (2010) The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site. FEBS Lett 584(11):2237-41 |
| abstractText | 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. |
