Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 28, Issue 4, Pages 210-214Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/S0968-0004(03)00057-4
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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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