Disulfide bonds as switches for protein function

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 solub...

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Bibliographic Details
Published in:Trends in biochemical sciences (Amsterdam. Regular ed.) 2003-04, Vol.28 (4), p.210-214
Main Author: Hogg, Philip J.
Format: Article
Language:English
Subjects:
CD4 Antigens - chemistry
Disulfides - chemistry
Disulfides - metabolism
Humans
Protein Structure, Secondary
Receptors, Cell Surface - chemistry
Receptors, Cell Surface - metabolism
Sulfhydryl Compounds - metabolism
Thrombospondin 1 - chemistry
Thrombospondin 1 - metabolism
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Summary: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.
ISSN:0968-0004
1362-4326
DOI:10.1016/S0968-0004(03)00057-4