Disulfide bonds as switches for protein function.
نویسنده
چکیده
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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ورودعنوان ژورنال:
- Trends in biochemical sciences
دوره 28 4 شماره
صفحات -
تاریخ انتشار 2003