IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v491y2012i7422d10.1038_nature11500.html
   My bibliography  Save this article

The spatial architecture of protein function and adaptation

Author

Listed:
  • Richard N. McLaughlin Jr

    (Green Center for Systems Biology, University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center
    Present address: Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109-1024, USA.)

  • Frank J. Poelwijk

    (Green Center for Systems Biology, University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

  • Arjun Raman

    (Green Center for Systems Biology, University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

  • Walraj S. Gosal

    (Green Center for Systems Biology, University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

  • Rama Ranganathan

    (Green Center for Systems Biology, University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

Abstract

A high-throughput mutagenesis study in a PDZ domain shows that biochemical function and adaptation primarily originate from a collectively evolving amino acid network within the structure termed a protein sector.

Suggested Citation

  • Richard N. McLaughlin Jr & Frank J. Poelwijk & Arjun Raman & Walraj S. Gosal & Rama Ranganathan, 2012. "The spatial architecture of protein function and adaptation," Nature, Nature, vol. 491(7422), pages 138-142, November.
  • Handle: RePEc:nat:nature:v:491:y:2012:i:7422:d:10.1038_nature11500
    DOI: 10.1038/nature11500
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature11500
    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/nature11500?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. Ahmed Abdul Quadeer & David Morales-Jimenez & Matthew R McKay, 2018. "Co-evolution networks of HIV/HCV are modular with direct association to structure and function," PLOS Computational Biology, Public Library of Science, vol. 14(9), pages 1-29, September.
    2. Khaled Daqrouq & Rami Alhmouz & Ahmed Balamesh & Adnan Memic, 2015. "Application of Wavelet Transform for PDZ Domain Classification," PLOS ONE, Public Library of Science, vol. 10(4), pages 1-16, April.
    3. Alistair Bailey & Andy van Hateren & Tim Elliott & Jörn M Werner, 2014. "Two Polymorphisms Facilitate Differences in Plasticity between Two Chicken Major Histocompatibility Complex Class I Proteins," PLOS ONE, Public Library of Science, vol. 9(2), pages 1-11, February.
    4. Tiberiu Teşileanu & Lucy J Colwell & Stanislas Leibler, 2015. "Protein Sectors: Statistical Coupling Analysis versus Conservation," PLOS Computational Biology, Public Library of Science, vol. 11(2), pages 1-20, February.
    5. Emily K. Makowski & Patrick C. Kinnunen & Jie Huang & Lina Wu & Matthew D. Smith & Tiexin Wang & Alec A. Desai & Craig N. Streu & Yulei Zhang & Jennifer M. Zupancic & John S. Schardt & Jennifer J. Lin, 2022. "Co-optimization of therapeutic antibody affinity and specificity using machine learning models that generalize to novel mutational space," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    6. Bian Li & Dan M. Roden & John A. Capra, 2022. "The 3D mutational constraint on amino acid sites in the human proteome," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    7. Willow Coyote-Maestas & David Nedrud & Antonio Suma & Yungui He & Kenneth A. Matreyek & Douglas M. Fowler & Vincenzo Carnevale & Chad L. Myers & Daniel Schmidt, 2021. "Probing ion channel functional architecture and domain recombination compatibility by massively parallel domain insertion profiling," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    8. Shou-Wen Wang & Anne-Florence Bitbol & Ned S Wingreen, 2019. "Revealing evolutionary constraints on proteins through sequence analysis," PLOS Computational Biology, Public Library of Science, vol. 15(4), pages 1-16, April.

    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:491:y:2012:i:7422:d:10.1038_nature11500. 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.