Disulfide bonds as switches for protein function.

@article{Hogg2003DisulfideBA,
  title={Disulfide bonds as switches for protein function.},
  author={Philip J Hogg},
  journal={Trends in biochemical sciences},
  year={2003},
  volume={28 4},
  pages={210-4}
}
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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Disulfide exchange in domain 2 of CD4 is required for entry of the human immunodeficiency virus type 1

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  • Nat. Immun
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Inhibitors of protein disulfide isomerase (PDI) prevent cleavage of disulfide-bonds in receptor-bound gp120 and prevent HIV-1

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