Format

Send to

Choose Destination
Trends Biochem Sci. 2003 Apr;28(4):210-4.

Disulfide bonds as switches for protein function.

Author information

1
Centre for Vascular Research, University of New South Wales, and Department of Haematology, Prince of Wales Hospital, NSW, Australia. p.hogg@unsw.edu.au

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.

PMID:
12713905
DOI:
10.1016/S0968-0004(03)00057-4
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center