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 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.
Hogg
Philip J
PJ
Centre for Vascular Research, University of New South Wales, and Department of Haematology, Prince of Wales Hospital, NSW, Australia. p.hogg@unsw.edu.au
D015704:CD4 Antigens / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D017433:Protein Structure, Secondary; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism; D013438:Sulfhydryl Compounds / Q000378:metabolism; D019700:Thrombospondin 1 / Q000737:chemistry / Q000378:metabolism
D015704:CD4 Antigens; D004220:Disulfides; D011956:Receptors, Cell Surface; D013438:Sulfhydryl Compounds; D019700:Thrombospondin 1