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Review
. 2005 Dec;15(6):646-51.
doi: 10.1016/j.sbi.2005.10.001. Epub 2005 Oct 24.

Allosteric regulation of chaperonins

Amnon Horovitz  1 , Keith R Willison
Affiliations
Review

Allosteric regulation of chaperonins

Amnon Horovitz et al. Curr Opin Struct Biol. 2005 Dec.

Abstract

Chaperonins are molecular machines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space by complex allosteric regulation. Recently, progress has been made in describing the various functional (allosteric) states of these machines, the pathways by which they interconvert, and the coupling between allosteric transitions and protein folding reactions. However, various mechanistic issues remain to be resolved.

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