IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v551y2017i7681d10.1038_nature24627.html
   My bibliography  Save this article

Structure of the human MHC-I peptide-loading complex

Author

Listed:
  • Andreas Blees

    (Institute of Biochemistry, Biocenter, Goethe University Frankfurt)

  • Dovile Januliene

    (Max Planck Institute of Biophysics)

  • Tommy Hofmann

    (Interdisciplinary Research Center HALOmen, Martin Luther University Halle-Wittenberg)

  • Nicole Koller

    (Institute of Biochemistry, Biocenter, Goethe University Frankfurt)

  • Carla Schmidt

    (Interdisciplinary Research Center HALOmen, Martin Luther University Halle-Wittenberg)

  • Simon Trowitzsch

    (Institute of Biochemistry, Biocenter, Goethe University Frankfurt)

  • Arne Moeller

    (Max Planck Institute of Biophysics)

  • Robert Tampé

    (Institute of Biochemistry, Biocenter, Goethe University Frankfurt)

Abstract

Electron cryo-microscopy structures of the human peptide-loading complex shed light on its operation and on the onset of adaptive immune responses.

Suggested Citation

  • Andreas Blees & Dovile Januliene & Tommy Hofmann & Nicole Koller & Carla Schmidt & Simon Trowitzsch & Arne Moeller & Robert Tampé, 2017. "Structure of the human MHC-I peptide-loading complex," Nature, Nature, vol. 551(7681), pages 525-528, November.
    • Handle: RePEc:nat:nature:v:551:y:2017:i:7681:d:10.1038_nature24627
    DOI: 10.1038/nature24627
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature24627
    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/nature24627?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. Lenong Li & Xubiao Peng & Mansoor Batliwala & Marlene Bouvier, 2023. "Crystal structures of MHC class I complexes reveal the elusive intermediate conformations explored during peptide editing," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Jiansheng Jiang & Daniel K. Taylor & Ellen J. Kim & Lisa F. Boyd & Javeed Ahmad & Michael G. Mage & Hau V. Truong & Claire H. Woodward & Nikolaos G. Sgourakis & Peter Cresswell & David H. Margulies & , 2022. "Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    3. Alexander Domnick & Christian Winter & Lukas Sušac & Leon Hennecke & Mario Hensen & Nicole Zitzmann & Simon Trowitzsch & Christoph Thomas & Robert Tampé, 2022. "Molecular basis of MHC I quality control in the peptide loading complex," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    4. Xin Lei & Indu Khatri & Tom Wit & Iris Rink & Marja Nieuwland & Ron Kerkhoven & Hans Eenennaam & Chong Sun & Abhishek D. Garg & Jannie Borst & Yanling Xiao, 2023. "CD4+ helper T cells endow cDC1 with cancer-impeding functions in the human tumor micro-environment," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    5. Ines Katharina Müller & Christian Winter & Christoph Thomas & Robbert M. Spaapen & Simon Trowitzsch & Robert Tampé, 2022. "Structure of an MHC I–tapasin–ERp57 editing complex defines chaperone promiscuity," Nature Communications, Nature, vol. 13(1), pages 1-10, 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:551:y:2017:i:7681:d:10.1038_nature24627. 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.