A new twist to coiled coil. - Inserm - Institut national de la santé et de la recherche médicale Access content directly
Journal Articles FEBS Letters Year : 2012

A new twist to coiled coil.


Spectrin repeats have been largely considered as passive linkers or spacers with little functional role other than to convey flexibility to a protein. Whilst this is undoubtedly part of their function, it is by no means all. Whilst the overt structure of all spectrin repeats is a simple triple-helical coiled coil, the linkages between repeats and the surface properties of repeats vary widely. Spectrin repeats in different proteins can act as dimerisation interfaces, platforms for the recruitment of signalling molecules, and as a site for the interaction with cytoskeletal elements and even direct association with membrane lipids. In the case of dystrophin several of these functions overlap in the space of a few repeats.
Fichier principal
Vignette du fichier
New-Twist-OpenAccess-CC-BY.pdf (1.26 Mo) Télécharger le fichier
Origin Explicit agreement for this submission

Dates and versions

inserm-00700015 , version 1 (05-09-2013)



Elisabeth Le Rumeur, Jean-François Hubert, Steve J. Winder. A new twist to coiled coil.. FEBS Letters, 2012, 586 (17), pp.2717-2722. ⟨10.1016/j.febslet.2012.05.004⟩. ⟨inserm-00700015⟩
123 View
242 Download



Gmail Mastodon Facebook X LinkedIn More