Proteins that switch folds.

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TitleProteins that switch folds.
Publication TypeJournal Article
Year of Publication2010
AuthorsBryan, PN, Orban, J
JournalCurr Opin Struct Biol
Volume20
Issue4
Pagination482-8
Date Published2010 Aug
ISSN1879-033X
KeywordsAnimals, Humans, Protein Conformation, Protein Folding, Protein Stability, Proteins
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.

DOI10.1016/j.sbi.2010.06.002
Alternate JournalCurr. Opin. Struct. Biol.
PubMed ID20591649
PubMed Central IDPMC2928869
Grant ListGM62154 / GM / NIGMS NIH HHS / United States
R01 GM062154-07 / GM / NIGMS NIH HHS / United States