1SJ8

Solution Structure of the R1R2 Domains of Talin

Summary for 1SJ8

• Entry DOI: 10.2210/pdb1sj8/pdb
• Related: 1SJ7
• Descriptor: Talin 1 (2 entities in total)
• Functional Keywords: structural protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P26039
• Total number of polymer chains: 1
• Total formula weight: 31512.32

Authors

Papagrigoriou, E.,Gingras, A.R.,Barsukov, I.L.,Critchley, D.R.,Emsley, J. (deposition date: 2004-03-03, release date: 2004-08-24, Last modification date: 2023-08-23)

Primary citation

Papagrigoriou, E.,Gingras, A.R.,Barsukov, I.L.,Bate, N.,Fillingham, I.J.,Patel, B.,Frank, R.,Ziegler, W.H.,Roberts, G.C.,Critchley, D.R.,Emsley, J.
Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle
EMBO J., 23:2942-2951, 2004

PubMed Abstract: 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.

PubMed: 15272303
DOI: 10.1038/sj.emboj.7600285

Experimental method

X-RAY DIFFRACTION (2.6 Å)