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FEBS Lett. 2012 Aug 14;586(17):2717-22. doi: 10.1016/j.febslet.2012.05.004. Epub 2012 May 11.

A new twist to coiled coil.

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1
Université Européenne de Bretagne, 35000 Rennes, France.

Abstract

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.

PMID:
22584055
DOI:
10.1016/j.febslet.2012.05.004
[Indexed for MEDLINE]
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