The domain structure of talin: Residues 1815–1973 form a five-helix bundle containing a cryptic vinculin-binding site
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.
Structured summary
MINT-7722300, MINT-7760951: Talin-1 (uniprotkb:P26039) and Vinculin (uniprotkb:P12003) bind (MI:0407) by molecular sieving (MI:0071)
Abbreviations: HSQC, heteronuclear single quantum coherence, SCOP, structural classification of proteins, VBS, vinculin-binding site
Keywords: Talin, Vinculin, NMR, Domain structure, Helical bundle
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PII: S0014-5793(10)00298-X
doi:10.1016/j.febslet.2010.04.028
© 2010 Federation of European Biochemical Societies
