Sandbox Reserved 1100

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The Adiponectin receptor 1 is an integral membrane protein composed of 375 amino acids and its molecular weight is 42,4 kDa. This protein can be decomposed into different parts: an internal <scene name='82/829353/N-terminus_domain/2'>N-terminus domain</scene> (residues 89 to 120), a short intracellular domain called <scene name='82/829353/Helice0/2'>helix 0</scene> (residues 121 to 129), <scene name='82/829353/7helices/1'>seven transmembrane helices</scene> (residues 134 to 364) and an external <scene name='82/829353/C-terminus_domain/3'>C-terminus domain</scene> (residues 365 to 375). <ref name="doc1"/>
The Adiponectin receptor 1 is an integral membrane protein composed of 375 amino acids and its molecular weight is 42,4 kDa. This protein can be decomposed into different parts: an internal <scene name='82/829353/N-terminus_domain/2'>N-terminus domain</scene> (residues 89 to 120), a short intracellular domain called <scene name='82/829353/Helice0/2'>helix 0</scene> (residues 121 to 129), <scene name='82/829353/7helices/1'>seven transmembrane helices</scene> (residues 134 to 364) and an external <scene name='82/829353/C-terminus_domain/3'>C-terminus domain</scene> (residues 365 to 375). <ref name="doc1"/>
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The organisation of the structure of the Adiponectin receptor 1 is the opposite to [[G protein-coupled receptor]] family. Indeed, the Adiponectin receptor has an internal <scene name='82/829353/N-terminus_domain/2'>N-terminus domain</scene> and an external <scene name='82/829353/C-terminus_domain/3'>C-terminus domain</scene> while the G-protein family has an internal N-terminus domain and an external C-terminus domain. <ref name="doc3"> Takashi Kadowaki and Toshimasa Yamauchi et al. « Adiponectin and adiponectin receptors». https://www.ncbi.nlm.nih.gov/pubmed/15897298</ref> <ref name="doc1"/> <ref name="doc5"> Parker-Duffen JL, Nakamura K, Silver M, Zuriaga MA, MacLauchlan S, Aprahamian TR, Walsh K et al. «Divergent roles for adiponectin receptor 1 (AdipoR1) and AdipoR2 in mediating revascularization and metabolic dysfunction in vivo.» 17 April 2014 : https://www.ncbi.nlm.nih.gov/pubmed/24742672<ref/>
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The organisation of the structure of the Adiponectin receptor 1 is the opposite to [[G protein-coupled receptor]] family. Indeed, the Adiponectin receptor has an internal <scene name='82/829353/N-terminus_domain/2'>N-terminus domain</scene> and an external <scene name='82/829353/C-terminus_domain/3'>C-terminus domain</scene> while the G-protein family has an internal N-terminus domain and an external C-terminus domain. <ref name="doc3"> Takashi Kadowaki and Toshimasa Yamauchi et al. « Adiponectin and adiponectin receptors». https://www.ncbi.nlm.nih.gov/pubmed/15897298</ref> <ref name="doc1"/> <ref name="doc5"> Parker-Duffen JL, Nakamura K, Silver M, Zuriaga MA, MacLauchlan S, Aprahamian TR, Walsh K et al. «Divergent roles for adiponectin receptor 1 (AdipoR1) and AdipoR2 in mediating revascularization and metabolic dysfunction in vivo.» 17 April 2014 : https://www.ncbi.nlm.nih.gov/pubmed/24742672</ref>
The Adiponectin receptor 1 contains <scene name='82/829353/7helices/1'>seven transmembrane helices</scene> linked thanks to three extracellular loops and three intracellular loops. The <scene name='82/829353/Helix1/2'>helix I</scene> is formed by the residues 135 to 157, <scene name='82/829353/Helix2/2'>helix II</scene> by the residues 169 to 192, the <scene name='82/829353/Helix3/2'>helix III</scene> by the residues 198 to 227, the <scene name='82/829353/Helix4/2'>helice IV</scene> by the residues 232 to 252, the <scene name='82/829353/Helice5/2'>helix V</scene> by the residues 264 to 288 <scene name='82/829353/Helix6/2'>heliX VI</scene> by the residues 305 to 319 and the <scene name='82/829353/Helix7/2'>helix VII</scene> by the residues 336 to 364 .Besides, the <scene name='82/829353/Helix3/2'>helix III</scene> and <scene name='82/829353/Helix7/2'>VII</scene> are longer than the other helices. These <scene name='82/829353/7tm/2'>seven transmembrane helices</scene> have a clockwise circular specific organisation (from helix I to helix VII) and form a bundle.
The Adiponectin receptor 1 contains <scene name='82/829353/7helices/1'>seven transmembrane helices</scene> linked thanks to three extracellular loops and three intracellular loops. The <scene name='82/829353/Helix1/2'>helix I</scene> is formed by the residues 135 to 157, <scene name='82/829353/Helix2/2'>helix II</scene> by the residues 169 to 192, the <scene name='82/829353/Helix3/2'>helix III</scene> by the residues 198 to 227, the <scene name='82/829353/Helix4/2'>helice IV</scene> by the residues 232 to 252, the <scene name='82/829353/Helice5/2'>helix V</scene> by the residues 264 to 288 <scene name='82/829353/Helix6/2'>heliX VI</scene> by the residues 305 to 319 and the <scene name='82/829353/Helix7/2'>helix VII</scene> by the residues 336 to 364 .Besides, the <scene name='82/829353/Helix3/2'>helix III</scene> and <scene name='82/829353/Helix7/2'>VII</scene> are longer than the other helices. These <scene name='82/829353/7tm/2'>seven transmembrane helices</scene> have a clockwise circular specific organisation (from helix I to helix VII) and form a bundle.
Concerning the extracellular faces, the three extracellular loops which connect the transmembrane helices are exposed and it is the same for the <scene name='82/829353/C-terminus_domain/3'>C-terminus domain</scene>. Besides, <scene name='82/829353/Helix3/2'>helix III</scene> and the <scene name='82/829353/Helix7/2'>VII</scene> are longer than the other helices and as a result the <scene name='82/829353/C-terminus_domain/3'>C-terminus domain</scene> two turns of the <scene name='82/829353/Helix7/2'>VII</scene> are exposed too. <ref name="doc1"/>
Concerning the extracellular faces, the three extracellular loops which connect the transmembrane helices are exposed and it is the same for the <scene name='82/829353/C-terminus_domain/3'>C-terminus domain</scene>. Besides, <scene name='82/829353/Helix3/2'>helix III</scene> and the <scene name='82/829353/Helix7/2'>VII</scene> are longer than the other helices and as a result the <scene name='82/829353/C-terminus_domain/3'>C-terminus domain</scene> two turns of the <scene name='82/829353/Helix7/2'>VII</scene> are exposed too. <ref name="doc1"/>

Revision as of 20:19, 15 January 2020

This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115.
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The AdipoR1 receptor

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References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. ↑ 3.0 3.1 3.2 3.3 3.4 Tanabe, Hiroaki, Yoshifumi Fujii, Miki Okada-Iwabu, Masato Iwabu, Yoshihiro Nakamura, Toshiaki Hosaka, Kanna Motoyama, et al. « Crystal structures of the human adiponectin receptors ». Nature 520, nᵒ 7547 (1 avril 2015): 312‑16. https://doi.org/10.1038/nature14301
  4. ↑ 4.0 4.1 4.2 Kadowaki, Takashi et al. “Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome.” The Journal of clinical investigation vol. 116,7 (2006): 1784-92. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1483172/
  5. ↑ 5.0 5.1 5.2 Whitehead, J. P., A. A. Richards, I. J. Hickman, G. A. Macdonald, et J. B. Prins. « Adiponectin – a Key Adipokine in the Metabolic Syndrome ». Diabetes, Obesity and Metabolism 8, nᵒ 3 (2006): 264‑80. https://doi.org/10.1111/j.1463-1326.2005.00510.x.
  6. ↑ 6.0 6.1 Yamauchi, Toshimasa, Junji Kamon, Yusuke Ito, Atsushi Tsuchida, Takehiko Yokomizo, Shunbun Kita, Takuya Sugiyama, et al. « Cloning of adiponectin receptors that mediate antidiabetic metabolic effects ». Nature 423, nᵒ 6941 (1 juin 2003): 762‑69. https://doi.org/10.1038/nature01705.
  7. ↑ 7.0 7.1 Takashi Kadowaki and Toshimasa Yamauchi et al. « Adiponectin and adiponectin receptors». https://www.ncbi.nlm.nih.gov/pubmed/15897298
  8. ↑ Parker-Duffen JL, Nakamura K, Silver M, Zuriaga MA, MacLauchlan S, Aprahamian TR, Walsh K et al. «Divergent roles for adiponectin receptor 1 (AdipoR1) and AdipoR2 in mediating revascularization and metabolic dysfunction in vivo.» 17 April 2014 : https://www.ncbi.nlm.nih.gov/pubmed/24742672
  9. ↑ Kosel D, Heiker JT, Juhl C, Wottawah CM, Blüher M, Mörl K, Beck-Sickinger AG et al. « Dimerization of adiponectin 1 is inhibited by adiponectin » Journal of Cell Science 123, 1320-1328 : https://www.ncbi.nlm.nih.gov/pubmed/20332107
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