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Trends Biochem Sci. 2012 Dec;37(12):517-25. doi: 10.1016/j.tibs.2012.08.006. Epub 2012 Sep 24.

Conditional disorder in chaperone action.

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1
Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109, USA.

Abstract

Protein disorder remains an intrinsically fuzzy concept. Its role in protein function is difficult to conceptualize and its experimental study is challenging. Although a wide variety of roles for protein disorder have been proposed, establishing that disorder is functionally important, particularly in vivo, is not a trivial task. Several molecular chaperones have now been identified as conditionally disordered proteins; fully folded and chaperone-inactive under non-stress conditions, they adopt a partially disordered conformation upon exposure to distinct stress conditions. This disorder appears to be vital for their ability to bind multiple aggregation-sensitive client proteins and to protect cells against the stressors. The study of these conditionally disordered chaperones should prove useful in understanding the functional role for protein disorder in molecular recognition.

PMID:
23018052
PMCID:
PMC3508372
DOI:
10.1016/j.tibs.2012.08.006
[Indexed for MEDLINE]
Free PMC Article
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