PMID: identifiant
de la référence Pubmed : |
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 (22584055) |
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| titre : |
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A new twist to coiled coil. |
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| auteur(s) : |
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Elisabeth Le Rumeur1, Jean-François Hubert1, Steve Winder ( ) 2 |
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| laboratoire : |
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| Équipe de recherche : |
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Equipe Structures et Interactions Moléculaires |
| résumé : |
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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. |
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| domaine : |
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langue du texte
intégral : |
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Anglais |
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| ISSN : |
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1873-3468 |
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| type de publication : |
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Articles dans des revues avec comité de lecture |
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| DOI : |
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10.1016/j.febslet.2012.05.004 |
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| journal : |
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FEBS Lett |
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| Audience : |
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internationale |
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| date de publication : |
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11/05/2012 |
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date de publication
électronique : |
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11/05/2012 |
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| page, identifiant, ... : |
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epub ahead of print |
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| mots-clés auteur : |
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α-Actinin – Dystrophin – Spectrin – Spectrin repeat – Plakins – Plectin – Nesprin – Coiled-coil – Phospholipid – Sarcolemma – Duchenne muscular dystrophy |
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