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Coiled coils meet the chaperone world

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Martin,  J       
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Protein Folding, Unfolding and Degradation Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Gruber,  M
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Lupas,  AN       
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Martin, J., Gruber, M., & Lupas, A. (2004). Coiled coils meet the chaperone world. Trends in biochemical sciences, 29(9), 455-458. doi:10.1016/j.tibs.2004.07.004.


Cite as: https://hdl.handle.net/21.11116/0000-000B-3A21-F
Abstract
Coiled coils are versatile structural modules that engage in a variety of cellular activities. Recent studies illuminate their role as substrate-binding elements in the chaperone cofactor prefoldin and in the AAA+ ATPases involved in protein (un)folding processes. The use of coiled coils to mediate the binding of non-native proteins represents a novel strategy in chaperone design and a new function for coiled coils.