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Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/3330

Title: A vinculin-binding domain from the talin rod unfolds to form a complex with the vinculin head
Authors: Fillingham, Ian
Gingras, Alexandre R.
Papagrigoriou, Evangelos
Patel, Bipin
Emsley, Jonas
Critchley, David R.
Roberts, Gordon C.K.
Barsukov, Igor L.
Issue Date: 11-Jan-2005
Publisher: Elsevier (Cell Press)
Citation: Structure, 2005, 13 (1), pp. 65-74
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 β-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 4-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 unrecognised VBSs.
DOI Link: 10.1016/j.str.2004.11.006
ISSN: 0969-2126
Links: http://hdl.handle.net/2381/3330
http://www.sciencedirect.com/science/article&(...)
Version: Post print
Status: Peer reviewed
Type: Article
Rights: © 2005 Elsevier Ltd. Deposited with reference to the publisher’s archiving policy available on the SHERPA/RoMEO website.
Appears in Collections:Published Articles, Dept. of Biochemistry

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