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

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...

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Detalles Bibliográficos
Autores principales: Goult, Benjamin T., Gingras, Alexandre R., Bate, Neil, Barsukov, Igor L., Critchley, David R., Roberts, Gordon C.K.
Formato: Texto
Lenguaje:English
Publicado: Elsevier Science B.V 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2887493/
https://www.ncbi.nlm.nih.gov/pubmed/20399778
http://dx.doi.org/10.1016/j.febslet.2010.04.028
Descripción
Sumario: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)

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