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

Sangwon Lee, Jungyuen Choi, Jyotidarsini Mohanty, Leiliane P. Sousa, Francisco Tome, Els Pardon, Jan Steyaert, Mark A. Lemmon, Irit Lax and Joseph Schlessinger ()
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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

Nature, 2018, vol. 553, issue 7689, 501-505

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.

Date: 2018
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DOI: 10.1038/nature25010

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