1U6H

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

Summary for 1U6H

• Entry DOI: 10.2210/pdb1u6h/pdb
• Descriptor: Vinculin, Talin (3 entities in total)
• Functional Keywords: protein-protein complex, cell adhesion
• Biological source: Gallus gallus (chicken); More
• Cellular location: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : P12003
• Total number of polymer chains: 2
• Total formula weight: 34460.74

Authors

Fillingham, I.,Gingras, A.R.,Papagrigoriou, E.,Patel, B.,Emsley, J.,Roberts, G.C.K.,Critchley, D.R.,Barsukov, I.L. (deposition date: 2004-07-30, release date: 2005-01-18, Last modification date: 2024-04-03)

Primary citation

Fillingham, I.,Gingras, A.R.,Papagrigoriou, E.,Patel, B.,Emsley, J.,Critchley, D.R.,Roberts, G.C.,Barsukov, I.L.
A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head.
Structure, 13:65-74, 2005

PubMed 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.

PubMed: 15642262
DOI: 10.1016/j.str.2004.11.006

Experimental method

X-RAY DIFFRACTION (2.38 Å)