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I24-Microfocus Macromolecular Crystallography	Crystal structures of the human adiponectin receptors Hiroaki Tanabe , Yoshifumi Fujii , Miki Okada-Iwabu , Masato Iwabu , Yoshihiro Nakamura , Toshiaki Hosaka , Kanna Motoyama , Mariko Ikeda , Motoaki Wakiyama , Takaho Terada , Noboru Ohsawa , Masakatsu Hato , Satoshi Ogasawara , Tomoya Hino , Takeshi Murata , So Iwata , Kunio Hirata , Yoshiaki Kawano , Masaki Yamamoto , Tomomi Kimura-Someya Nature 520, 312 - 316 DOI: 10.1038/nature14301 PMID: 25855295 Show Abstract ▼ Abstract: Adiponectin stimulation of its receptors, AdipoR1 and AdipoR2, increases the activities of 5′ AMP-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor (PPAR), respectively, thereby contributing to healthy longevity as key anti-diabetic molecules. AdipoR1 and AdipoR2 were predicted to contain seven transmembrane helices with the opposite topology to G-protein-coupled receptors. Here we report the crystal structures of human AdipoR1 and AdipoR2 at 2.9 and 2.4 Å resolution, respectively, which represent a novel class of receptor structure. The seven-transmembrane helices, conformationally distinct from those of G-protein-coupled receptors, enclose a large cavity where three conserved histidine residues coordinate a zinc ion. The zinc-binding structure may have a role in the adiponectin-stimulated AMPK phosphorylation and UCP2 upregulation. Adiponectin may broadly interact with the extracellular face, rather than the carboxy-terminal tail, of the receptors. The present information will facilitate the understanding of novel structure–function relationships and the development and optimization of AdipoR agonists for the treatment of obesity-related diseases, such as type 2 diabetes.	Apr 2015

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I24-Microfocus Macromolecular Crystallography

Crystal structures of the human adiponectin receptors