Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/14517
Title: A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head.
Authors: Fillingham, I
Gingras, AR
Papagrigoriou, E
Patel, B
Emsley, J
Critchley, DR
Roberts, GC
Barsukov, IL
First Published: Jan-2005
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 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.
DOI Link: 10.1016/j.str.2004.11.006
ISSN: 0969-2126
Links: http://hdl.handle.net/2381/14517
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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