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Curr Opin Struct Biol. 2010 Aug;20(4):482-8. doi: 10.1016/j.sbi.2010.06.002. Epub 2010 Jun 28.

Proteins that switch folds.

Author information

1
Institute for Bioscience and Biotechnology Research, Department of Bioengineering, University of Maryland, 9600 Gudelsky Drive, Rockville, MD 20850, USA. bryan@umbi.umd.edu

Abstract

An increasing number of proteins demonstrate the ability to switch between very different fold topologies, expanding their functional utility through new binding interactions. Recent examples of fold switching from naturally occurring and designed systems have a number of common features: (i) The structural transitions require states with diminished stability; (ii) Switching involves flexible regions in one conformer or the other; (iii) A new binding surface is revealed in the alternate fold that can lead to both stabilization of the alternative state and expansion of biological function. Fold switching not only provides insight into how new folds evolve, but also indicates that an amino acid sequence has more information content than previously thought. A polypeptide chain can encode a stable fold while simultaneously hiding latent propensities for alternative states with novel functions.

PMID:
20591649
PMCID:
PMC2928869
DOI:
10.1016/j.sbi.2010.06.002
[Indexed for MEDLINE]
Free PMC Article

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