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|Title: ||A vinculin-binding domain from the talin rod unfolds to form a complex with the vinculin head|
|Authors: ||Fillingham, Ian|
Gingras, Alexandre R.
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|
|Version: ||Post print|
|Status: ||Peer reviewed|
|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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