6krz

Crystal structure of the human adiponectin receptor 1 D208A mutant

spinqualitylabelsall models 6krz, resolution 3.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6krz is a 9 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.05Å Ligands: OLA, OLB, PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAQR1_HUMAN Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:12802337, PubMed:25855295). Required for normal glucose and fat homeostasis and for maintaining a normal body weight. ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis. Has high affinity for globular adiponectin and low affinity for full-length adiponectin (By similarity).[UniProtKB:Q91VH1] Publication Abstract from PubMed The human adiponectin receptors, AdipoR1 and AdipoR2, are key anti-diabetic molecules. We previously reported the crystal structures of human AdipoR1 and AdipoR2, revealing that their seven transmembrane helices form an internal closed cavity (the closed form). In this study, we determined the crystal structure of the D208A variant AdipoR1, which is fully active with respect to the major downstream signaling. Among the three molecules in the asymmetric unit, two assume the closed form, and the other adopts the open form with large openings in the internal cavity. Between the closed- and open-form structures, helices IV and V are tilted with their intracellular ends shifted by about 4 and 11 A, respectively. Furthermore, we reanalyzed our previous wild-type AdipoR1 diffraction data, and determined a 44:56 mixture of the closed and open forms, respectively. Thus, we have clarified the closed-open interconversion of AdipoR1, which may be relevant to its functional mechanism(s). Human adiponectin receptor AdipoR1 assumes closed and open structures.,Tanabe H, Fujii Y, Okada-Iwabu M, Iwabu M, Kano K, Kawana H, Hato M, Nakamura Y, Terada T, Kimura-Someya T, Shirouzu M, Kawano Y, Yamamoto M, Aoki J, Yamauchi T, Kadowaki T, Yokoyama S Commun Biol. 2020 Aug 14;3(1):446. doi: 10.1038/s42003-020-01160-4. PMID:32796916 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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