The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site.



Goult, Benjamin T ORCID: 0000-0002-3438-2807, Gingras, Alexandre R ORCID: 0000-0002-5373-0176, Bate, Neil, Barsukov, Igor L, Critchley, David R and Roberts, Gordon CK ORCID: 0000-0001-6200-1373
(2010) The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site. FEBS letters, 584 (11). pp. 2237-2241.

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Abstract

Talin is a large flexible rod-shaped protein that activates the integrin family of cell adhesion molecules and couples them to cytoskeletal actin. Its rod region consists of a series of helical bundles. Here we show that residues 1815-1973 form a 5-helix bundle, with a topology unique to talin which is optimally suited for formation of a long rod such as talin. This is much more stable than the 4-helix (1843-1973) domain described earlier and as a result its vinculin binding sequence is inaccessible to vinculin at room temperature, with implications for the overall mechanism of the talin-vinculin interaction.

Item Type: Article
Uncontrolled Keywords: Cytoskeleton, Animals, Mice, Actins, Talin, Vinculin, Integrins, Binding Sites, Protein Structure, Secondary, Protein Binding
Divisions: Faculty of Health and Life Sciences
Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology
Depositing User: Symplectic Admin
Date Deposited: 13 Mar 2024 09:31
Last Modified: 13 Mar 2024 09:31
DOI: 10.1016/j.febslet.2010.04.028
Related URLs:
URI: https://livrepository.liverpool.ac.uk/id/eprint/3179355