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

Masaharu Aritomi, Naoki Kunishima, Tomoyuki Okamoto, Ryota Kuroki, Yoshimi Ota and Kosuke Morikawa ()
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Masaharu Aritomi: Biomolecular Engineering Research Institute
Naoki Kunishima: Biomolecular Engineering Research Institute
Tomoyuki Okamoto: Biomolecular Engineering Research Institute
Ryota Kuroki: Central Laboratories for Key Technology, Kirin Brewery Co. Ltd
Yoshimi Ota: Biomolecular Engineering Research Institute
Kosuke Morikawa: Biomolecular Engineering Research Institute

Nature, 1999, vol. 401, issue 6754, 713-717

Abstract: 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.

Date: 1999
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DOI: 10.1038/44394

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