IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v501y2013i7466d10.1038_nature12443.html
   My bibliography  Save this article

Computational design of ligand-binding proteins with high affinity and selectivity

Author

Listed:
  • Christine E. Tinberg

    (University of Washington)

  • Sagar D. Khare

    (University of Washington
    Present address: Department of Chemistry and Chemical Biology, Center for Integrative Proteomics Research, Rutgers University, Piscataway, New Jersey 08854, USA.)

  • Jiayi Dou

    (University of Washington
    Graduate Program in Biological Physics, Structure, and Design, University of Washington)

  • Lindsey Doyle

    (Fred Hutchinson Cancer Research Center)

  • Jorgen W. Nelson

    (University of Washington)

  • Alberto Schena

    (Ecole Polytechnique Fédérale de Lausanne, Institute of Chemical Sciences and Engineering, Institute of Bioengineering, National Centre of Competence in Research (NCCR) in Chemical Biology, 1015 Lausanne, Switzerland)

  • Wojciech Jankowski

    (Center for Integrative Proteomics Research, Rutgers University)

  • Charalampos G. Kalodimos

    (Center for Integrative Proteomics Research, Rutgers University)

  • Kai Johnsson

    (Ecole Polytechnique Fédérale de Lausanne, Institute of Chemical Sciences and Engineering, Institute of Bioengineering, National Centre of Competence in Research (NCCR) in Chemical Biology, 1015 Lausanne, Switzerland)

  • Barry L. Stoddard

    (Fred Hutchinson Cancer Research Center)

  • David Baker

    (University of Washington
    Howard Hughes Medical Institute, University of Washington)

Abstract

Computational protein design is used to create a protein that binds the steroid digoxigenin (DIG) with high affinity and selectivity; the computational design methods described here should help to enable the development of a new generation of small molecule receptors for synthetic biology, diagnostics and therapeutics.

Suggested Citation

  • Christine E. Tinberg & Sagar D. Khare & Jiayi Dou & Lindsey Doyle & Jorgen W. Nelson & Alberto Schena & Wojciech Jankowski & Charalampos G. Kalodimos & Kai Johnsson & Barry L. Stoddard & David Baker, 2013. "Computational design of ligand-binding proteins with high affinity and selectivity," Nature, Nature, vol. 501(7466), pages 212-216, September.
  • Handle: RePEc:nat:nature:v:501:y:2013:i:7466:d:10.1038_nature12443
    DOI: 10.1038/nature12443
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature12443
    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/nature12443?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. Namrata Anand & Raphael Eguchi & Irimpan I. Mathews & Carla P. Perez & Alexander Derry & Russ B. Altman & Po-Ssu Huang, 2022. "Protein sequence design with a learned potential," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Betz, Ulrich A.K. & Arora, Loukik & Assal, Reem A. & Azevedo, Hatylas & Baldwin, Jeremy & Becker, Michael S. & Bostock, Stefan & Cheng, Vinton & Egle, Tobias & Ferrari, Nicola & Schneider-Futschik, El, 2023. "Game changers in science and technology - now and beyond," Technological Forecasting and Social Change, Elsevier, vol. 193(C).
    3. Wojciech Jankowski & Stepan S. Surov & Nancy E. Hernandez & Atul Rawal & Marcos Battistel & Daron Freedberg & Mikhail V. Ovanesov & Zuben E. Sauna, 2024. "Engineering and evaluation of FXa bypassing agents that restore hemostasis following Apixaban associated bleeding," Nature Communications, Nature, vol. 15(1), pages 1-9, 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:501:y:2013:i:7466:d:10.1038_nature12443. 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.