IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v450y2007i7172d10.1038_nature06524.html
   My bibliography  Save this article

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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature06524
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature06524?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. 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.
    2. 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.
    3. 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.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:450:y:2007:i:7172:d:10.1038_nature06524. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.