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The origin of protein interactions and allostery in colocalization

Author

Listed:
  • John Kuriyan

    (Howard Hughes Medical Institute, California Institute for Quantitative Biosciences, University of California
    Lawrence Berkeley National Laboratory)

  • David Eisenberg

    (Howard Hughes Medical Institute, Institute of Molecular Biology, University of California)

Abstract

Two fundamental principles can account for how regulated networks of interacting proteins originated in cells. These are the law of mass action, which holds that the binding of one molecule to another increases with concentration, and the fact that the colocalization of molecules vastly increases their local concentrations. It follows that colocalization can amplify the effect on one protein of random mutations in another protein and can therefore, through natural selection, lead to interactions between proteins and to a startling variety of complex allosteric controls. It also follows that allostery is common and that homologous proteins can have different allosteric mechanisms. Thus, the regulated protein networks of organisms seem to be the inevitable consequence of natural selection operating under physical laws.

Suggested Citation

  • John Kuriyan & David Eisenberg, 2007. "The origin of protein interactions and allostery in colocalization," Nature, Nature, vol. 450(7172), pages 983-990, December.
  • Handle: RePEc:nat:nature:v:450:y:2007:i:7172:d:10.1038_nature06524
    DOI: 10.1038/nature06524
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    Cited by:

    1. Yalbi Itzel Balderas-Martínez & Michael Savageau & Heladia Salgado & Ernesto Pérez-Rueda & Enrique Morett & Julio Collado-Vides, 2013. "Transcription Factors in Escherichia coli Prefer the Holo Conformation," PLOS ONE, Public Library of Science, vol. 8(6), pages 1-9, June.
    2. Ashfaq Ur Rehman & Shah Saud & Nasir Ahmad & Abdul Wadood & R Hamid, 2017. "Allosteric regulation in drug design," Current Trends in Biomedical Engineering & Biosciences, Juniper Publishers Inc., vol. 4(1), pages 9-11, May.
    3. Robert Kalescky & Hongyu Zhou & Jin Liu & Peng Tao, 2016. "Rigid Residue Scan Simulations Systematically Reveal Residue Entropic Roles in Protein Allostery," PLOS Computational Biology, Public Library of Science, vol. 12(4), pages 1-21, April.

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