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Review
. 2015 Oct;1850(10):1973-82.
doi: 10.1016/j.bbagen.2014.12.019. Epub 2014 Dec 24.

Control of protein function by prolyl isomerization

Philipp A M Schmidpeter  1 , Johanna R Koch  1 , Franz X Schmid  2
Affiliations
Review

Control of protein function by prolyl isomerization

Philipp A M Schmidpeter et al. Biochim Biophys Acta. 2015 Oct.

Abstract

Background: Prolyl cis/trans isomerizations have long been known as critical and rate-limiting steps in protein folding.

Results: Now it is clear that they are also used as slow conformational switches and molecular timers in the regulation of protein activity. Here we describe several such proline switches and how they are regulated.

Conclusions and general significance: Prolyl isomerizations can function as attenuators and provide allosteric systems with a molecular memory. This article is part of a Special Issue entitled Proline-directed Foldases: Cell Signaling Catalysts and Drug Targets.

Keywords: Allostery; Prolyl isomerase; Protein folding; Protein regulation; Signaling.

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