Disulfide Bonds As Switches for Protein Function

Overview

Journal Trends Biochem Sci

Specialty Biochemistry

Date 2003 Apr 26

PMID 12713905

Citations 187

Authors

Philip J Hogg

Affiliations

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Abstract

The prevailing view is that disulfide bonds have been added during evolution to enhance the stability of proteins that function in a fluctuating cellular environment. However, recent evidence indicates that disulfide bonds can be more than inert structural motifs. The function of some secreted soluble proteins and cell-surface receptors is controlled by cleavage of one or more of their disulfide bonds; this cleavage is mediated by catalysts or facilitators that are specific for their substrate.

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