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Allosteric regulation of proteins

A historical perspective on the development of concepts and techniques

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Abstract

Allostery is a mechanism by which the activity of a large number of proteins is regulated. It is manifested as a change in the activity, either ligand binding or catalysis of one site of a protein due to a ligand binding to another distinct site of the protein. The allosteric effect is transduced by a change in the structural properties of the protein. It has been traditionally understood using either the concerted MWC (Monod, Wyman and Changeux) model, or the sequential KNF (Koshland, Nemethy and Filmer) model of structural changes. However, allostery is fundamentally a thermodynamic process and requires an alteration in the enthalpy or entropy associated with the process.

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Suggested Reading

  1. Q Cui and M Karplus, Allostery and Cooperativity Revisited, Protein Sci., Vol.17, No.8, pp.1295–307, 2008.

    Article  Google Scholar 

  2. A W Fenton, Allostery: An Illustrated Definition for the ‘Second Secret of Life’, Trends Biochem Sci., Vol.33, No.9, pp.420–5, 2008.

    Article  Google Scholar 

  3. C J Tsai, A Del Sol and R Nussinov, Protein Allostery, Signal Transmission and Dynamics: A Classification Scheme of Allosteric Mechanisms, Mol Biosyst, Vol.5, No.3, pp.207–16, 2009.

    Article  Google Scholar 

  4. A Cooper and D T Dryden, Allostery Without Conformational Change–A Plausible Model, Eur. Biophys. J, Vol.11, No.2, pp.103–9, 1984.

    Article  Google Scholar 

  5. C J Tsai, A Del Sol and R Nussinov, Allostery: Absence of a Change in Shape Does Not Imply that Allostery is Not at Play, J Mol. Biol., Vol.378, No.1, pp.1–11, 2008.

    Article  Google Scholar 

  6. C Bohr, K A Hasselback and A Krogh, Über einen in biologischen Beziehung wichtigen Einfluss, den die Kohlen-sauerspannung des Blutes auf dessen Sauerstoffbindung bt, Skand. Arch. Physiol., Vol.15, pp.401–412, 1904.

    Article  Google Scholar 

  7. H E Umbarger, Evidence for a Negative-feedback Mechanism in the Biosynthesis of Isoleucine, Science, Vol.123, No.3202, p.848, 1956.

    Article  Google Scholar 

  8. A B Pardee and R A Yates, Control of Pyrimidine Biosynthesis in Escherichia coli by a Feed-Back Mechanism, J Biol Chem., Vol.221, No.2, pp.757–70, 1956.

    Google Scholar 

  9. J Monod and F Jacob, Teleonomic Mechanisms in Cellular Metabolism, Growth, and Differentiation, Cold Spring Harb Symp Quant Biol., Vol.26, pp.389–401, 1961.

    Article  Google Scholar 

  10. J Monod, J Wyman and J P Changeux, On the Nature of Allosteric Transitions: A Plausible Model, J. Mol. Biol., Vol.12, pp.88–118, 1965.

    Article  Google Scholar 

  11. D E Koshland, Jr., G Nemethy and D Filmer, Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits, Biochemistry, Vol.5, No.1, pp.365–85, 1966.

    Article  Google Scholar 

  12. J D Bryngelson and P G Wolynes, Spin Glasses and the Statistical Mechanics of Protein Folding, Proc. Natl. Acad. Sci., USA, Vol.84, No.21, pp.7524–8, 1987.

    Article  Google Scholar 

  13. J N Onuchic, Z Luthey-Schulten and P G Wolynes, Theory of Protein Folding: The Energy Landscape Perspective, Annu. Rev. Phys. Chem., Vol.48, pp.545–600, 1997.

    Article  Google Scholar 

  14. H Ishikawa et al., Direct Observation of Fast Protein Conformational Switching, Proc. Natl. Acad. Sci., USA, Vol.105, No.25, pp.8619–24, 2008.

    Article  Google Scholar 

  15. P T Zhuravlev and G A Papoian, Protein Functional Landscapes, Dynamics, Allostery: A Tortuous Path Towards a Universal Theoretical Framework, Q Rev. Biophys., Vol.43, No.3, pp.1–38, 2010.

    Article  Google Scholar 

  16. P Csermely, R Palotai and R Nussinov, Induced-fit, Conformational Selection and Independent Dynamic Segments: An Extended View of Binding Events, Trends Biochem Sci., Vol.35, No.10, pp.539–546, 2010.

    Article  Google Scholar 

  17. N Popovych et al., Dynamically Driven Protein Allostery, Nat Struct Mol Biol., Vol.13, No.9, pp.831–8, 2006.

    Article  Google Scholar 

  18. S R Tzeng and C G Kalodimos, Dynamic Activation of an Allosteric Regulatory Protein, Nature, Vol.462, No.7271, pp.368–72, 2009.

    Article  Google Scholar 

  19. K H Biswas, S Sopory and S S Visweswariah, The GAF Domain of the cGMPbinding, cGMP-specific phosphodiesterase (PDE5) is a sensor and a sink for cGMP, Biochemistry, Vol.47, No.11, pp.3534–43, 2008.

    Article  Google Scholar 

  20. K H Biswas and S S Visweswariah, Distinct Allostery Induced in the Cyclic GMP-binding, Cyclic GMP-Specific Phosphodiesterase (PDE5) by Cyclic GMP, Sildenafil, and metal ions, J Biol. Chem., Vol.286, No.10, pp.8545–54, 2011.

    Article  Google Scholar 

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Authors and Affiliations

  1. Department of Molecular Reproduction Development and Genetics Biology Building GA09, Indian Institute of Science, Bengaluru, 560 012, India

    Kabir H. Biswas

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  1. Kabir H. Biswas
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Correspondence to Kabir H. Biswas.

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Kabir H Biswas is currently a Senior Research Fellow at the Mechanobiology Institute, National University of Singapore. His interest lies in studying how proteins are regulated by chemical or physical factors and is currently studying the organization of protein complexes on the cell membrane.

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Biswas, K.H. Allosteric regulation of proteins. Reson 22, 37–50 (2017). https://doi.org/10.1007/s12045-017-0431-z

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  • DOI: https://doi.org/10.1007/s12045-017-0431-z

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