A new twist to coiled coil

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• 作者：Elisabeth Le Rumeur ; Jean-Fran?ois Hubert ; Steve J. Winder
• 关键词：¦Á-Actinin ; Dystrophin ; Spectrin ; Spectrin repeat ; Plakins ; Plectin ; Nesprin ; Coiled-coil ; Phospholipid ; Sarcolemma ; Duchenne muscular dystrophy
• 刊名：FEBS Letters
• 出版年：2012
• 出版时间：14 August, 2012
• 年：2012
• 卷：586
• 期：17
• 页码：2717-2722
• 全文大小：1285 K

文摘

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.