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Folding of Disulfide Proteins pp 151–182Cite as

Allosteric Disulfide Bonds

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Part of the book series: Protein Reviews ((PRON,volume 14))

Abstract

Protein disulfide bonds link cysteine residues in the polypeptide chain. The bonds contribute, sometimes crucially, to protein stability and function and are strongly conserved through the evolution of species. By analyzing the conservation of all structurally validated disulfide bonds across 29 completely sequenced eukaryotic genomes, we found that disulfide-bonded cysteines are even more conserved than tryptophan – the most conserved amino acid. Moreover, the rate of acquisition of disulfide bonds shows a strong positive correlation with organism complexity, which probably reflects the requirement for more sophistication in protein function in complex species. The majority of disulfide bonds perform a structural role by stabilizing the mature protein. Some disulfide bonds perform a functional role in the mature protein and can be divided into catalytic or allosteric disulfides. Catalytic disulfides/dithiols transfer electrons between proteins, while the allosteric bonds control the function of the protein in which they reside when they break and/or form. There are currently a dozen or so examples of allosteric disulfide bonds. The features of these bonds and their involvement in the respective proteins’ function are discussed. A common aspect of 11 of the 12 allosteric bonds discussed herein is that they link β-strands or β-loops.

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Abbreviations

β2GPI:

β2-glycoprotein I

Csk:

Carboxyl-terminal Src kinase

ERp5:

Endoplasmic reticulum protein 5

GFP:

Green fluorescent protein

HIV:

Human immunodeficiency virus

MHCI:

Major histocompatibility complex class I

NK:

Natural killer

PDI:

Protein disulfide isomerase

TG2:

Transglutaminase 2

VWC:

von Willebrand factor type C domains

VWF:

von Willebrand factor

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Authors and Affiliations

  1. Lowy Cancer Research Centre, Prince of Wales Clinical School, University of New South Wales, 2052, Sydney, Australia

    Jason W. H. Wong & Philip J. Hogg

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  1. Jason W. H. Wong
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  2. Philip J. Hogg
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Correspondence to Philip J. Hogg .

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  1. Brown Foundation Inst. of Molecular Medi, The University of Texas, Houston, 77030, Texas, USA

    Rowen J. Y. Chang

  2. Institut de Biotecnologia i de Biomed., Dept. de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Bellaterra, 08193, Spain

    Salvador Ventura

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© 2011 Springer Science+Business Media, LLC

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Wong, J.W.H., Hogg, P.J. (2011). Allosteric Disulfide Bonds. In: Chang, R., Ventura, S. (eds) Folding of Disulfide Proteins. Protein Reviews, vol 14. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-7273-6_8

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