1sj7
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Crystal Structure of Talin Rod 482-655
OverviewOverview
The interaction between the cytoskeletal proteins talin and vinculin plays, a key role in integrin-mediated cell adhesion and migration. We have, determined the crystal structures of two domains from the talin rod, spanning residues 482-789. Talin 482-655, which contains a, vinculin-binding site (VBS), folds into a five-helix bundle whereas talin, 656-789 is a four-helix bundle. We show that the VBS is composed of a, hydrophobic surface spanning five turns of helix 4. All the key side, chains from the VBS are buried and contribute to the hydrophobic core of, the talin 482-655 fold. We demonstrate that the talin 482-655 five-helix, bundle represents an inactive conformation, and mutations that disrupt the, hydrophobic core or deletion of helix 5 are required to induce an active, conformation in which the VBS is exposed. We also report the crystal, structure of the N-terminal vinculin head domain in complex with an, activated form of talin. Activation of the VBS in talin and the, recruitment of vinculin may support the maturation of small integrin/talin, complexes into more stable adhesions.
About this StructureAbout this Structure
1SJ7 is a Single protein structure of sequence from Mus musculus with PT as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle., Papagrigoriou E, Gingras AR, Barsukov IL, Bate N, Fillingham IJ, Patel B, Frank R, Ziegler WH, Roberts GC, Critchley DR, Emsley J, EMBO J. 2004 Aug 4;23(15):2942-51. Epub 2004 Jul 22. PMID:15272303
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