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Disulfide bonds as switches for protein function
1Centre for Vascular Research, University of New South Wales, and Department of Haematology, Prince of Wales Hospital, NSW, Australia. p.hogg@unsw.edu.au
Trends in Biochemical Sciences
|April 26, 2003
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.