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Targeting allosteric disulphide bonds in cancer
1Lowy Cancer Research Centre and Prince of Wales Clinical School, University of New South Wales, Sydney NSW 2052, Australia. p.hogg@unsw.edu.au
Abstract:
Protein action in nature is generally controlled by the amount of protein produced and by chemical modification of the protein, and both are often perturbed in cancer. The amino acid side chains and the peptide and disulphide bonds that bind the polypeptide backbone can be post-translationally modified. Post-translational cleavage or the formation of disulphide bonds are now being identified in cancer-related proteins and it is timely to consider how these allosteric bonds could be targeted for new therapies.
Insights
Protein modifications like cleavage and disulphide bonds are altered in cancer. Targeting these allosteric bonds offers potential new cancer therapies.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
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