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Targeting allosteric disulphide bonds in cancer

Nature Reviews Cancer volume 13, pages 425–431 (2013)Cite this article

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A Corrigendum to this article was published on 03 June 2013

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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.

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Figure 1: The three basic types of post- translational modifications.
Figure 2: Mechanisms of cleavage of allosteric disulphide bonds.
Figure 3: Targeting allosteric disulphide bonds with small molecules.

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Change history

  • 13 May 2013

    This has now been corrected in the HTML and PDF versions of the article.

  • 03 June 2013

    In Table 1 of this article, the β3 integrin row should have read "523–544 and 560–583" in the "Disulphide cysteines" column and "−RHstaple and −LHhook (3IJE)" in the "Disulphide bond configuration (PDB identifiers)" column. This has been corrected online.

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Acknowledgements

This work was supported by grants from the National Health and Medical Research Council of Australia and the Cancer Council New South Wales.

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  1. Philip J. Hogg is at the Lowy Cancer Research Centre and Prince of Wales Clinical School, University of New South Wales, Sydney NSW 2052, Australia.,

    Philip J. Hogg

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Hogg, P. Targeting allosteric disulphide bonds in cancer. Nat Rev Cancer 13, 425–431 (2013). https://doi.org/10.1038/nrc3519

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