Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering
CHAPTER 2.3: Allosteric Disulfide Bonds
Published:27 Jul 2018
Special Collection: 2018 ebook collectionSeries: Chemical Biology
A. E. Pijning and P. J. Hogg, in Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering, ed. M. J. Feige, The Royal Society of Chemistry, 2018, pp. 152-174.
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Allosteric disulfides are a subset of disulfide bonds that control the function of the protein in which they reside when cleaved or formed. A conformational signature for these bonds is emerging and the reasons for their facile nature are being uncovered. The bonds are often naturally strained owing to local topological features, which facilitates their cleavage and has likely contributed to their evolution as allosteric disulfides. Biological processes that are controlled by this post-translational modification include hemostasis, immune response and viral infection. The allosteric bonds themselves and the factors that cleave them are being targeted for the treatment of disease.