Disulfide bonds as switches for protein function
PJ Hogg - Trends in biochemical sciences, 2003 - cell.com
Trends in biochemical sciences, 2003•cell.com
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.
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.
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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