IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v462y2009i7271d10.1038_nature08560.html
   My bibliography  Save this article

Dynamic activation of an allosteric regulatory protein

Author

Listed:
  • Shiou-Ru Tzeng

    (Department of Chemistry & Chemical Biology,
    Rutgers University, Piscataway, New Jersey 08854, USA)

  • Charalampos G. Kalodimos

    (Department of Chemistry & Chemical Biology,
    Rutgers University, Piscataway, New Jersey 08854, USA)

Abstract

Allostery goes dynamic Effector molecules are thought to control the activity of allosteric proteins by binding to an allosteric site, distinct from the active site, thereby inducing and stabilizing a specific conformational state of the protein. A new study suggests that the notion of purely structurally regulated activity in allosteric proteins should be revised to include a frequently dominating contribution from protein dynamics. Shiou-Ru Tzeng and Charalampos Kalodimos characterized cyclic AMP binding to catabolite activator protein (CAP), a transcriptional activator often used as a model for allostery. They find, surprisingly, that even when in a structurally inactive conformation, CAP can be activated for ligand (DNA) binding by changes in protein dynamics.

Suggested Citation

  • Shiou-Ru Tzeng & Charalampos G. Kalodimos, 2009. "Dynamic activation of an allosteric regulatory protein," Nature, Nature, vol. 462(7271), pages 368-372, November.
    • Handle: RePEc:nat:nature:v:462:y:2009:i:7271:d:10.1038_nature08560
    DOI: 10.1038/nature08560
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature08560
    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/nature08560?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. Federica Maschietto & Uriel N. Morzan & Florentina Tofoleanu & Aria Gheeraert & Apala Chaudhuri & Gregory W. Kyro & Peter Nekrasov & Bernard Brooks & J. Patrick Loria & Ivan Rivalta & Victor S. Batist, 2023. "Turning up the heat mimics allosteric signaling in imidazole-glycerol phosphate synthase," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Yuan Liang & Yunkai Qie & Jing Yang & Ranfeng Wu & Shuang Cui & Yuliang Zhao & Greg J. Anderson & Guangjun Nie & Suping Li & Cheng Zhang, 2023. "Programming conformational cooperativity to regulate allosteric protein-oligonucleotide signal transduction," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    3. Anna C. Papageorgiou & Michaela Pospisilova & Jakub Cibulka & Raghib Ashraf & Christopher A. Waudby & Pavel Kadeřávek & Volha Maroz & Karel Kubicek & Zbynek Prokop & Lumir Krejci & Konstantinos Tripsi, 2023. "Recognition and coacervation of G-quadruplexes by a multifunctional disordered region in RECQ4 helicase," Nature Communications, Nature, vol. 14(1), pages 1-19, December.

    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:462:y:2009:i:7271:d:10.1038_nature08560. 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.