| First Author | Fillingham I | Year | 2005 |
| Journal | Structure | Volume | 13 |
| Issue | 1 | Pages | 65-74 |
| PubMed ID | 15642262 | Mgi Jnum | J:247412 |
| Mgi Id | MGI:5926537 | Doi | 10.1016/j.str.2004.11.006 |
| Citation | Fillingham I, et al. (2005) A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head. Structure 13(1):65-74 |
| abstractText | The cytoskeletal protein talin plays a key role in activating integrins and in coupling them to the actin cytoskeleton. Its N-terminal globular head, which binds beta integrins, is linked to an extended rod having a C-terminal actin binding site and several vinculin binding sites (VBSs). The NMR structure of residues 755-889 of the rod (containing a VBS) is shown to be an amphipathic four-helix bundle with a left-handed topology. A talin peptide corresponding to the VBS binds the vinculin head; the X-ray crystallographic structure of this complex shows that the residues which interact with vinculin are buried in the hydrophobic core of the talin fragment. NMR shows that the interaction involves a major structural change in the talin fragment, including unfolding of one of its helices, making the VBS accessible to vinculin. Interestingly, the talin 755-889 fragment binds more than one vinculin head molecule, suggesting that the talin rod may contain additional as yet unrecognized VBSs. |
