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Atomic structure of the GCSF–receptor complex showing a new cytokine–receptor recognition scheme

Author

Listed:
  • Masaharu Aritomi

    (Biomolecular Engineering Research Institute
    Asahi Chemical Industry Co. Ltd)

  • Naoki Kunishima

    (Biomolecular Engineering Research Institute)

  • Tomoyuki Okamoto

    (Biomolecular Engineering Research Institute
    Central Laboratories for Key Technology, Kirin Brewery Co. Ltd)

  • Ryota Kuroki

    (Central Laboratories for Key Technology, Kirin Brewery Co. Ltd)

  • Yoshimi Ota

    (Biomolecular Engineering Research Institute
    Toray Industrial, Inc.)

  • Kosuke Morikawa

    (Biomolecular Engineering Research Institute)

Abstract

Granulocyte colony-stimulating factor (GCSF) is the principal growth factor regulating the maturation, proliferation and differentiation of the precursor cells of neutrophilic granulocytes1 and is used to treat neutropenia2. GCSF is a member of the long-chain subtype of the class 1 cytokine superfamily, which includes growth hormone, erythropoietin, interleukin 6 and oncostatin M (ref. 3). Here we have determined the crystal structure of GCSF complexed to the BN–BC domains, the principal ligand-binding region of the GCSF receptor (GCSFR). The two receptor domains form a complex in a 2:2 ratio with the ligand, with a non-crystallographic pseudo-twofold axis through primarily the interdomain region and secondarily the BC domain. This structural view of a gp130-type receptor–ligand complex presents a new molecular basis for cytokine–receptor recognition.

Suggested Citation

  • Masaharu Aritomi & Naoki Kunishima & Tomoyuki Okamoto & Ryota Kuroki & Yoshimi Ota & Kosuke Morikawa, 1999. "Atomic structure of the GCSF–receptor complex showing a new cytokine–receptor recognition scheme," Nature, Nature, vol. 401(6754), pages 713-717, October.
    • Handle: RePEc:nat:nature:v:401:y:1999:i:6754:d:10.1038_44394
    DOI: 10.1038/44394
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    Cited by:

    1. Julia Skokowa & Birte Hernandez Alvarez & Murray Coles & Malte Ritter & Masoud Nasri & Jérémy Haaf & Narges Aghaallaei & Yun Xu & Perihan Mir & Ann-Christin Krahl & Katherine W. Rogers & Kateryna Maks, 2022. "A topological refactoring design strategy yields highly stable granulopoietic proteins," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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