1u6h

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1u6h, resolution 2.38Å

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Vinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)

Overview

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.

About this Structure

1U6H is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.

Reference

A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head., Fillingham I, Gingras AR, Papagrigoriou E, Patel B, Emsley J, Critchley DR, Roberts GC, Barsukov IL, Structure. 2005 Jan;13(1):65-74. PMID:15642262

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