Literature DB >> 12713905

Disulfide bonds as switches for protein function.

Philip J Hogg1.   

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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Year:  2003        PMID： 12713905     DOI： 10.1016/S0968-0004(03)00057-4

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN： 0968-0004            Impact factor:   13.807


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