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Structures of β-klotho reveal a ‘zip code’-like mechanism for endocrine FGF signalling

Author

Listed:
  • Sangwon Lee

    (Yale School of Medicine)

  • Jungyuen Choi

    (Yale School of Medicine)

  • Jyotidarsini Mohanty

    (Yale School of Medicine)

  • Leiliane P. Sousa

    (Yale School of Medicine)

  • Francisco Tome

    (Yale School of Medicine)

  • Els Pardon

    (VIB Center for Structural Biology, Vrije Universiteit Brussel)

  • Jan Steyaert

    (VIB Center for Structural Biology, Vrije Universiteit Brussel)

  • Mark A. Lemmon

    (Yale School of Medicine)

  • Irit Lax

    (Yale School of Medicine)

  • Joseph Schlessinger

    (Yale School of Medicine)

Abstract

Crystal structures of free and ligand-bound β-klotho reveal that it acts as a primary receptor for FGF21, and demonstrate how a sugar-cutting enzyme has evolved to become a receptor for hormones that regulate metabolic processes.

Suggested Citation

  • Sangwon Lee & Jungyuen Choi & Jyotidarsini Mohanty & Leiliane P. Sousa & Francisco Tome & Els Pardon & Jan Steyaert & Mark A. Lemmon & Irit Lax & Joseph Schlessinger, 2018. "Structures of β-klotho reveal a ‘zip code’-like mechanism for endocrine FGF signalling," Nature, Nature, vol. 553(7689), pages 501-505, January.
    • Handle: RePEc:nat:nature:v:553:y:2018:i:7689:d:10.1038_nature25010
    DOI: 10.1038/nature25010
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