Skip to main content

Thank you for visiting You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

Crystal structures of the human adiponectin receptors

This article has been updated


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.

This is a preview of subscription content, access via your institution

Relevant articles

Open Access articles citing this article.

Access options

Rent or buy this article

Prices vary by article type



Prices may be subject to local taxes which are calculated during checkout

Figure 1: Overall structures of AdipoR1 and AdipoR2.
Figure 2: Sequence alignment of human AdipoR1 and AdipoR2.
Figure 3: The zinc-binding sites of AdipoR1 and AdipoR2.
Figure 4: The large internal cavities in the AdipoR1 and AdipoR2 structures.
Figure 5: The extracellular faces of AdipoR1 and AdipoR2.

Accession codes

Primary accessions

Protein Data Bank

Data deposits

The atomic coordinates and structure factors for the AdipoR1–Fv and AdipoR2–Fv structures have been deposited in the Protein Data Bank under the accession codes 3WXV and 3WXW, respectively.

Change history

  • 15 April 2015

    A minor editorial change was made to the legend of Figure 3 to recover the original label definition.


  1. Scherer, P. E., Williams, S., Fogliano, M., Baldini, G. & Lodish, H. F. A novel serum protein similar to C1q, produced exclusively in adipocytes. J. Biol. Chem. 270, 26746–26749 (1995)

    Article  CAS  Google Scholar 

  2. Hu, E., Liang, P. & Spiegelman, B. M. AdipoQ is a novel adipose-specific gene dysregulated in obesity. J. Biol. Chem. 271, 10697–10703 (1996)

    Article  CAS  Google Scholar 

  3. Maeda, K. et al. cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1). Biochem. Biophys. Res. Commun. 221, 286–289 (1996)

    Article  CAS  Google Scholar 

  4. Nakano, Y., Tobe, T., Choi-Miura, N. H., Mazda, T. & Tomita, M. Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma. J. Biochem. 120, 803–812 (1996)

    Article  CAS  Google Scholar 

  5. Hotta, K. et al. Plasma concentrations of a novel, adipose-specific protein, adiponectin, in type 2 diabetic patients. Arterioscler. Thromb. Vasc. Biol. 20, 1595–1599 (2000)

    Article  CAS  Google Scholar 

  6. Yamauchi, T. et al. The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity. Nature Med. 7, 941–946 (2001)

    Article  CAS  Google Scholar 

  7. Berg, A. H., Combs, T. P., Du, X., Brownlee, M. & Scherer, P. E. The adipocyte-secreted protein Acrp30 enhances hepatic insulin action. Nature Med. 7, 947–953 (2001)

    Article  CAS  Google Scholar 

  8. Fruebis, J. et al. Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice. Proc. Natl Acad. Sci. USA 98, 2005–2010 (2001)

    Article  ADS  CAS  Google Scholar 

  9. Yamauchi, T. et al. Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase. Nature Med. 8, 1288–1295 (2002)

    Article  CAS  Google Scholar 

  10. Tomas, E. et al. Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation. Proc. Natl Acad. Sci. USA 99, 16309–16313 (2002)

    Article  ADS  CAS  Google Scholar 

  11. Kahn, B. B., Alquier, T., Carling, D. & Hardie, D. G. AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. Cell Metab. 1, 15–25 (2005)

    Article  CAS  Google Scholar 

  12. Kersten, S., Desvergne, B. & Wahli, W. Roles of PPARs in health and disease. Nature 405, 421–424 (2000)

    Article  ADS  CAS  Google Scholar 

  13. Yamauchi, T. et al. Globular adiponectin protected ob/ob mice from diabetes and ApoE-deficient mice from atherosclerosis. J. Biol. Chem. 278, 2461–2468 (2003)

    Article  CAS  Google Scholar 

  14. Yamauchi, T. et al. Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature 423, 762–769 (2003)

    Article  ADS  CAS  Google Scholar 

  15. Wess, J. G-protein-coupled receptors: molecular mechanisms involved in receptor activation and selectivity of G-protein recognition. FASEB J. 11, 346–354 (1997)

    Article  CAS  Google Scholar 

  16. Yamauchi, T. et al. Targeted disruption of AdipoR1 and AdipoR2 causes abrogation of adiponectin binding and metabolic actions. Nature Med. 13, 332–339 (2007)

    Article  CAS  Google Scholar 

  17. Okada-Iwabu, M. et al. A small-molecule AdipoR agonist for type 2 diabetes and short life in obesity. Nature 503, 493–499 (2013)

    Article  ADS  CAS  Google Scholar 

  18. Lyons, T. J. et al. Metalloregulation of yeast membrane steroid receptor homologs. Proc. Natl Acad. Sci. USA 101, 5506–5511 (2004)

    Article  ADS  CAS  Google Scholar 

  19. Rasmussen, S. G. et al. Crystal structure of the human β2 adrenergic G-protein-coupled receptor. Nature 450, 383–387 (2007)

    Article  ADS  CAS  Google Scholar 

  20. Cherezov, V. et al. High-resolution crystal structure of an engineered human β2-adrenergic G protein-coupled receptor. Science 318, 1258–1265 (2007)

    Article  ADS  CAS  Google Scholar 

  21. Rosenbaum, D. M. et al. GPCR engineering yields high-resolution structural insights into β2-adrenergic receptor function. Science 318, 1266–1273 (2007)

    Article  ADS  CAS  Google Scholar 

  22. Rasmussen, S. G. et al. Structure of a nanobody-stabilized active state of the β2 adrenoceptor. Nature 469, 175–180 (2011)

    Article  ADS  CAS  Google Scholar 

  23. Rosenbaum, D. M. et al. Structure and function of an irreversible agonist-β2 adrenoceptor complex. Nature 469, 236–240 (2011)

    Article  ADS  CAS  Google Scholar 

  24. Venkatakrishnan, A. J. et al. Molecular signatures of G-protein-coupled receptors. Nature 494, 185–194 (2013)

    Article  ADS  CAS  Google Scholar 

  25. Rasmussen, S. G. et al. Crystal structure of the β2 adrenergic receptor-Gs protein complex. Nature 477, 549–555 (2011)

    Article  ADS  CAS  Google Scholar 

  26. Shimamura, T. et al. Structure of the human histamine H1 receptor complex with doxepin. Nature 475, 65–70 (2011)

    Article  CAS  Google Scholar 

  27. de Graaf, C. et al. Crystal structure-based virtual screening for fragment-like ligands of the human histamine H1 receptor. J. Med. Chem. 54, 8195–8206 (2011)

    Article  CAS  Google Scholar 

  28. Tanabe, H. et al. Expression, purification, crystallization, and preliminary X-ray crystallographic studies of the human adiponectin receptors, AdipoR1 and AdipoR2. J. Struct. Funct. Genomics 16, 11–23 (2015)

    Article  CAS  Google Scholar 

  29. Holm, L. & Rosenstrom, P. Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545–W549 (2010)

    Article  CAS  Google Scholar 

  30. Palczewski, K. et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289, 739–745 (2000)

    Article  ADS  CAS  Google Scholar 

  31. Pebay-Peyroula, E., Rummel, G., Rosenbusch, J. P. & Landau, E. M. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science 277, 1676–1681 (1997)

    Article  CAS  Google Scholar 

  32. Siu, F. Y. et al. Structure of the human glucagon class B G-protein-coupled receptor. Nature 499, 444–449 (2013)

    Article  ADS  CAS  Google Scholar 

  33. Wu, H. et al. Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator. Science 344, 58–64 (2014)

    Article  ADS  CAS  Google Scholar 

  34. Feng, L. et al. Structure of a site-2 protease family intramembrane metalloprotease. Science 318, 1608–1612 (2007)

    Article  ADS  CAS  Google Scholar 

  35. Bode, W., Gomis-Ruth, F. X., Huber, R., Zwilling, R. & Stocker, W. Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases. Nature 358, 164–167 (1992)

    Article  ADS  CAS  Google Scholar 

  36. Eriksson, A. E., Jones, T. A. & Liljas, A. Refined structure of human carbonic anhydrase II at 2.0 Å resolution. Proteins 4, 274–282 (1988)

    Article  CAS  Google Scholar 

  37. Mao, X. et al. APPL1 binds to adiponectin receptors and mediates adiponectin signalling and function. Nature Cell Biol. 8, 516–523 (2006)

    Article  CAS  Google Scholar 

  38. Hato, M., Hosaka, T., Tanabe, H., Kitsunai, T. & Yokoyama, S. A new manual dispensing system for in meso membrane protein crystallization with using a stepping motor-based dispenser. J. Struct. Funct. Genomics 15, 165–171 (2014)

    Article  CAS  Google Scholar 

  39. Hirata, K. et al. Achievement of protein micro-crystallography at SPring-8 beamline BL32XU. J. Phys. Conf. Ser. 425, 012002 (2013)

    Article  Google Scholar 

  40. Murakami, I. et al. Tumor volume and lymphovascular space invasion as a prognostic factor in early invasive adenocarcinoma of the cervix. J. Gynecol. Oncol. 23, 153–158 (2012)

    Article  Google Scholar 

  41. Ueno, G., Kanda, H., Kumasaka, T. & Yamamoto, M. Beamline Scheduling Software: administration software for automatic operation of the RIKEN structural genomics beamlines at SPring-8. J. Synchrotron Radiat. 12, 380–384 (2005)

    Article  Google Scholar 

  42. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307–326 (1997)

    Article  CAS  Google Scholar 

  43. Kabsch, W. Xds. Acta Crystallogr. D 66, 125–132 (2010)

    Article  CAS  Google Scholar 

  44. McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658–674 (2007)

    Article  CAS  Google Scholar 

  45. Terwilliger, T. C. Maximum-likelihood density modification. Acta Crystallogr. D 56, 965–972 (2000)

    Article  CAS  Google Scholar 

  46. Terwilliger, T. C. Automated side-chain model building and sequence assignment by template matching. Acta Crystallogr. D 59, 45–49 (2003)

    Article  Google Scholar 

  47. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486–501 (2010)

    Article  CAS  Google Scholar 

  48. Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213–221 (2010)

    Article  CAS  Google Scholar 

  49. Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12–21 (2010)

    Article  CAS  Google Scholar 

  50. DeLano, W. L. The PyMOL molecular graphics system. (DeLano Scientific, 2002)

    Google Scholar 

  51. Iwabu, M. et al. Adioponectin and AdipoR1 regulate PGC-1α and mitochondria by Ca2+ and AMPK/SIRT1. Nature 464, 1313–1319 (2010)

    Article  ADS  CAS  Google Scholar 

  52. Minokoshi, Y. et al. Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase. Nature 415, 339–343 (2002)

    Article  ADS  CAS  Google Scholar 

  53. Tsao, T. S., Murrey, H. E., Hug, C., Lee, D. H. & Lodish, H. F. Oligomerization state-dependent activation of NF-κB signaling pathway by adipocyte complement-related protein of 30 kDa (Acrp30). J. Biol. Chem. 277, 29359–29362 (2002)

    Article  CAS  Google Scholar 

  54. Woods, A., Salt, I., Scott, J., Hardie, D. G. & Carling, D. The α1 and α2 isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro . FEBS Lett. 397, 347–351 (1996)

    Article  CAS  Google Scholar 

  55. Hayashi, T. et al. Metabolic stress and altered glucose transport. Activation of AMP-activated protein kinase as a unifying coupling mechanism. Diabetes 49, 527–531 (2000)

    Article  CAS  Google Scholar 

  56. Hanson, M. A. et al. Crystal structure of a lipid G protein-coupled receptor. Science 335, 851–855 (2012)

    Article  ADS  CAS  Google Scholar 

  57. Lebon, G. et al. Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation. Nature 474, 521–525 (2011)

    Article  CAS  Google Scholar 

  58. Vogeley, L. et al. Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 Å. Science 306, 1390–1393 (2004)

    Article  ADS  CAS  Google Scholar 

Download references


We are grateful to the staffs of BL32XU at SPring-8 (proposals 2012A1332, 2012B1453, 2013A1008, 2013A1008, 2013B1034, 2013B1007, 2014A1007, 2014A1008 and 2014A1186), beamline I24 at Diamond Light Source, and beamline X06SA at the Swiss Light Source for their assistance in data collection. We thank R. Akasaka for protein analysis, M. Toyama, M. Inoue, M. Goto, M. Aoki and K. Ishii for expression plasmid preparation, M. Nishimoto, Y. Tomabechi and Y. Terazawa for technical assistance with protein expression and purification, and Y. Nishibaba, M. Yuasa and A. Hayashi for technical assistance and support with the activity assays of the mutants. This work was supported by grants from the Targeted Proteins Research Program (S.Y., T.K., S.I. and M.Y.), the Platform for Drug Discovery, Informatics and Structural Life Science (S.Y. and M.Y.), a Grant-in-Aid for Specially Promoted Research (26000012) (T.K.), Grants-in-Aid for Scientific Research (S) (20229008, 25221307) (T.K.), a Grant-in-Aid for Scientific Research (B) (26293216) (M.O.-I.), a Grant-in-Aid for Young Scientists (A) (30557236) (M. Iwabu), and the Translational Research Network Program (M.O.-I.), from the Ministry of Education, Culture, Sports, Science and Technology of Japan, by the research acceleration program of the Japan Science and Technology Agency (S.I.), and by the BBSRC (BB/G02325/1) (S.I.). The authors are grateful for the use of the Membrane Protein Laboratory funded by the Wellcome Trust (grant 062164/Z/00/Z) (S.I.) at the Diamond Light Source Limited.

Author information

Authors and Affiliations



H.T., T.K.-S., M.S., M.O.-I., M. Iwabu, T.Y., T.K. and S.Y. designed the research. H.T., K.M., M. Ikeda, M.W. and T.T. performed protein expression, purification and analyses of AdipoR1 and AdipoR2, while N.O. designed and constructed the expression plasmids. M.H. provided the lipidic mesophase crystallization techniques, and H.T. and K.M. performed the crystallization of the receptors. Y.F., H.T., Y.N. and T. Hosaka performed the X-ray diffraction data collection and the structural analysis. K.H., Y.K. and M.Y. optimized the microcrystal data collection strategy, using BL32XU at SPring-8. H.T. prepared the AdipoR1 and AdipoR2 immunogens, and H.T., K.M., S.O., T. Hino, T.M. and S.I. produced the anti-AdipoR1 monoclonal antibody. M.O.-I. and M. Iwabu assayed the activities of the mutants. H.T., T.K.-S., M.S., M.O.-I., M. Iwabu, T.Y., T.K. and S.Y. wrote the manuscript. All authors commented on the manuscript.

Corresponding authors

Correspondence to Toshimasa Yamauchi, Takashi Kadowaki or Shigeyuki Yokoyama.

Ethics declarations

Competing interests

The authors declare no competing financial interests.

Extended data figures and tables

Extended Data Figure 1 Analysis of N-terminal deletion mutants of AdipoR1 and AdipoR2 and lattice packing of the AdipoR1–Fv and AdipoR2–Fv crystals.

a, Phosphorylation and amounts of AMPK in HEK293 cells transfected with full-length AdipoR1 (residues 1–375) or N-terminally truncated mutants (residues 47–375, 77–375, 89–375, 102–375 and 120–375), treated for 5 min with adiponectin (15 μg ml−1). b, UCP2 mRNA levels in HEK293 cells transfected with full-length AdipoR2 (residues 1–386) or N-terminally truncated mutants (residues 88–386 and 100–386), treated for 18 h with adiponectin (3 μg ml−1). All values are mean ± s.e.m. n = 3–4, three independent experiments. **P < 0.01 compared to control cells or as indicated (see Methods for statistical tests used). NS, not significant. ch, Lattice packing of the AdipoR1–Fv crystals (ce) and the AdipoR2–Fv crystals (fh). AdipoR1, AdipoR2 and Fv are coloured green, cyan and grey, respectively. The AdipoR1–Fv and AdipoR2–Fv complexes crystallized with an anti-parallel arrangement of the receptor molecules.

Extended Data Figure 2 Comparison of the AdipoR1–Fv and AdipoR2–Fv structures.

ac, Superimposition of the AdipoR1–Fv and AdipoR2–Fv complexes: side view (a), extracellular view (b), intracellular view (c). Fv was omitted from the intracellular view for clarity. d, Superimposition of the subdomains consisting of helices I, II, III and VII between AdipoR1 and AdipoR2. The Cα r.m.s.d. value is 0.34 Å. e, Helix 0 (pink) interacts hydrophobically with the cytoplasmic ends of helices I–III, and the ICL1 (purple), as represented by those of AdipoR1. In addition, the zinc ion firmly connects helices VII, II and III (Fig. 3). Therefore, helices VII, I, II and III (d) constitute a rigid subdomain in the 7TM-domain structures. By contrast, helices IV, V and VI are superimposed between AdipoR1 and AdipoR2 with a Cα r.m.s.d. value of 0.73 Å, and are likely to constitute the other subdomain, with some conformational differences in helix V between AdipoR1 and AdipoR2.

Extended Data Figure 3 Comparison of the AdipoR2 structure with other 7TM proteins.

The structures of 7TM proteins in the N-terminus-out topology were inverted and superimposed on the AdipoR2 structure in the C-terminus-out topology. Superimpositions of AdipoR2 (cyan) with the β2AR (PDB code 2RH1) (r.m.s.d. 3.9 Å) (a), the glucagon receptor (PDB code 4L6R) (r.m.s.d. 3.8 Å) (b), the metabotropic glutamate receptor 1 (PDB code 4OR2) (r.m.s.d. 2.9 Å) (c), the sphingosine 1-phosphate receptor 1 (PDB code 3V2Y)56 (r.m.s.d. 3.0 Å) (d), the A2A adenosine receptor (PDB code 2YDV)57 (r.m.s.d. 3.4 Å) (e), and sensory rhodopsin (PDB code 1XIO)58 (r.m.s.d. 3.1 Å) (f) in orange. The AdipoR2 and other 7TM protein structures are viewed parallel to the membrane (top) and from the extracellular and intracellular sides, respectively (bottom).

Extended Data Figure 4 The zinc-binding sites of AdipoR1 and AdipoR2.

a, b, The zinc-binding sites of AdipoR1 (a) and AdipoR2 (b) are conserved from mammals to plants. The conserved residues, the 3× His+Asp residues and a Ser residue, are shown in red. The side chains of Ser 187 (AdipoR1) and Ser 198 (AdipoR2) in helix II are located 3.7 and 3.8 Å, respectively, away from the zinc ion (data not shown and Fig. 3b). c, d, The amounts of AdipoR1 (c) and AdipoR2 (d) in HEK293 cells transfected with AdipoR1 (residues 89–375), AdipoR2 (residues 100–386) or a variety of mutants of AdipoR1 and AdipoR2 were analysed by western blotting, using an anti-Flag antibody. The label 89–375 indicates no mutation, and the other labels, such as His191Ala and 4Ala, indicate the single and multiple mutations (see text). The label 100–386 indicates no mutation, and the other labels, such as His202Ala and 4Ala, indicate the single and multiple mutations (see text). e, UCP2 mRNA levels in HEK293 cells transfected with full-length AdipoR2 (residues 1–386) or a zinc-binding site mutant. All values are presented as mean ± s.e.m. n = 3–4, three independent experiments, *P < 0.05, **P < 0.01 compared to control cells or as indicated (see Methods).

Extended Data Figure 5 The zinc-binding sites of soluble proteins.

a, b, The zinc-binding sites of Astacus astacus L. astacin (PDB code 1AST) (a) and human carbonic anhydrase II (PDB code 1CA2) (b). The zinc ion (magenta) is coordinated by three His residues and a water molecule (pink sphere).

Extended Data Figure 6 The cytoplasmic side of AdipoR1.

a, b, Structures of AdipoR1 residues 89–375 (a) and 120–375 (b) viewed parallel to the membrane. c, d, The cavity of AdipoR1 (residues 89–375 (c) and 120–375 (d)) viewed from the cytoplasmic side. Residues 120–375, including helix 0, the 7TM domain, and the CTR, are coloured green. The NTR (residues 89–119) is coloured orange.

Extended Data Figure 7 The cytoplasmic faces of AdipoR2 and AdipoR1.

a, b, Intracellular views of AdipoR1 (a) and AdipoR2 (b). The openings of the cavities are circled in red. The N-terminal regions of the AdipoRs are represented as surface models (orange). c, d, The ICL2 s of AdipoR1 (c) and AdipoR2 (d).

Extended Data Figure 8 Crystal packing of the CTRs of AdipoR1 and AdipoR2.

a, b, Crystal packing of the CTR of AdipoR1 with Fv (a) and the CTR of AdipoR2 with Fv (b). The CTR of AdipoR1 is tucked between the two Fv fragments, whereas the C-terminal tail of AdipoR2 contacts the framework region 1 of VH (orange). The CTRs are coloured purple.

Extended Data Figure 9 Expression of the AdipoR1 mutant proteins.

a, b, The amounts of AdipoR1 in HEK293 cells transfected with full-length AdipoR1 (residues 1–375) or a variety of mutants of AdipoR1 were analysed by western blotting, using an anti-Flag antibody. Full-length AdipoR1 (residues 1–375) and the C-terminally truncated mutant (residues 1–370, 1–366 and 1–362) were used in a. AdipoR1 residues 1–375, MYFMAPL (residues 161–167) changed to SGSSGGS (ECL1); residues 1–375, YCS (residues 229–231) changed to GGG (ECL2); residues 1–375, FVKATTV (residues 291–297) changed to SSSGGGS (ECL3); residues 1–375, ECL1 and ECL3 (ECL1/3); and residues 1–375, ECL1, ECL2 and ECL3 (ECL1/2/3) were used in b.

Extended Data Table 1 Data collection and refinement statistics (Molecular replacement)

PowerPoint slides

Rights and permissions

Reprints and Permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Tanabe, H., Fujii, Y., Okada-Iwabu, M. et al. Crystal structures of the human adiponectin receptors. Nature 520, 312–316 (2015).

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI:

This article is cited by


By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.


Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing