6ks1

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Crystal structure of the human adiponectin receptor 2

Structural highlights

6ks1 is a 3 chain structure with sequence from Homo sapiens and Mus musculus. This structure supersedes the now removed PDB entry 3wxw. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:LPX, OLA, OLB, OLC, ZN
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PAQR2_HUMAN Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:12802337, PubMed:25855295). Required for normal body fat and glucose homeostasis. ADIPOQ-binding activates a signaling cascade that leads to increased PPARA activity, and ultimately to increased fatty acid oxidation and glucose uptake. Has intermediate affinity for globular and full-length adiponectin. Required for normal revascularization after chronic ischemia caused by severing of blood vessels (By similarity).[UniProtKB:Q8BQS5][1] [2]

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[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
6 reviews cite this structure
Sphingolipids in metabolic disease: The good, the bad, and the unknown.
Green et al. (2021)
5 more
5 other articles
No citations found

See Also

References

  1. ↑ Yamauchi T, Kamon J, Ito Y, Tsuchida A, Yokomizo T, Kita S, Sugiyama T, Miyagishi M, Hara K, Tsunoda M, Murakami K, Ohteki T, Uchida S, Takekawa S, Waki H, Tsuno NH, Shibata Y, Terauchi Y, Froguel P, Tobe K, Koyasu S, Taira K, Kitamura T, Shimizu T, Nagai R, Kadowaki T. Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature. 2003 Jun 12;423(6941):762-9. PMID:12802337 doi:http://dx.doi.org/10.1038/nature01705
  2. ↑ Tanabe H, Fujii Y, Okada-Iwabu M, Iwabu M, Nakamura Y, Hosaka T, Motoyama K, Ikeda M, Wakiyama M, Terada T, Ohsawa N, Hato M, Ogasawara S, Hino T, Murata T, Iwata S, Hirata K, Kawano Y, Yamamoto M, Kimura-Someya T, Shirouzu M, Yamauchi T, Kadowaki T, Yokoyama S. Crystal structures of the human adiponectin receptors. Nature. 2015 Apr 16;520(7547):312-6. doi: 10.1038/nature14301. Epub 2015 Apr 8. PMID:25855295 doi:http://dx.doi.org/10.1038/nature14301
  3. ↑ 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. Human adiponectin receptor AdipoR1 assumes closed and open structures. Commun Biol. 2020 Aug 14;3(1):446. PMID:32796916 doi:10.1038/s42003-020-01160-4

Contents


PDB ID 6ks1

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OCA

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