Sandbox Reserved 1100: Difference between revisions
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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"/> | ||
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 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"/> | ||
