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Comparative Study
. 2005 Jan;13(1):65-74.
doi: 10.1016/j.str.2004.11.006.

A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head

Ian Fillingham  1 , Alexandre R Gingras, Evangelos Papagrigoriou, Bipin Patel, Jonas Emsley, David R Critchley, Gordon C K Roberts, Igor L Barsukov
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Free article
Comparative Study

A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head

Ian Fillingham et al. Structure. 2005 Jan.
Free article

Abstract

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.

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