Structural asymmetry in FGF23 signaling

descriptionPublicationkeyboard_double_arrow_right Article 01 Dec 2023 English Publisher:Elsevier BVJournal:Trends in Pharmacological Sciences, volume 44, pages 862-864 (issn: 0165-6147,

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Authors: Shih-Hsien Liu; Zhousheng Xiao; Jeremy C. Smith; L. Darryl Quarles;

doi: 10.1016/j.tips.2023.09.005

pmid: 37778940

pmc: PMC11675616

Structural asymmetry in FGF23 signaling

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Abstract

Chen et al. have derived cryogenic electron microscopy (cryo-EM) structures of signaling complexes of the endocrine hormone fibroblast growth factor 23 (FGF23) with fibroblast growth factor receptor (FGFR), α-Klotho, and heparin sulfate. These structures are asymmetric, leading to questions concerning in vivo function, and will facilitate structure-based drug design to modulate FGF23 signaling.

Related Organizations

University of Tennessee at Knoxville
United States
Oak Ridge National Laboratory
United States
University of Tennessee Health Science Center
United States

Keywords

Fibroblast Growth Factors, Humans, Klotho Proteins, Receptors, Fibroblast Growth Factor, Glucuronidase, Signal Transduction

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