Review
doi: 10.1016/S0968-0004(03)00057-4.
Disulfide bonds as switches for protein function
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- PMID: 12713905
- DOI: 10.1016/S0968-0004(03)00057-4
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Review
Disulfide bonds as switches for protein function
Trends Biochem Sci.
2003 Apr.
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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