Sandbox Reserved 1100: Difference between revisions

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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.
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.
The Adiponectin receptor 1 contains <scene name='82/829353/7tm/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'>helix 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/Helix6/2'>VI</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'>helix 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/Helix6/2'>VI</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/Helix6/2'>VI</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 ??? protrude and are exposed too.
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/Helix6/2'>VI</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 ??? protrude and are exposed too.
The seven transmembrane helices surround a large internal cavity where a <scene name='82/829353/Zinc-binding_site/1'>zinc-binding site</scene> can be found. This cavity located from the cytoplasmic surface to the middle of the outer lipid layer of the membrane has small openings between the <scene name='82/829353/Helice5/2'>helix V</scene> and <scene name='82/829353/Helix6/2'>VI</scene>, and between the <scene name='82/829353/Helix4/2'>helix IV</scene> and <scene name='82/829353/Helix6/2'>VI</scene>. It has been assumed that these openings are involved in the entrance and exit of both substrate and product.
The seven transmembrane helices surround a large internal cavity where a <scene name='82/829353/Zinc-binding_site/1'>zinc-binding site</scene> can be found. This cavity located from the cytoplasmic surface to the middle of the outer lipid layer of the membrane has small openings between the <scene name='82/829353/Helice5/2'>helix V</scene> and <scene name='82/829353/Helix6/2'>VI</scene>, and between the <scene name='82/829353/Helix4/2'>helix IV</scene> and <scene name='82/829353/Helix6/2'>VI</scene>. It has been assumed that these openings are involved in the entrance and exit of both substrate and product.
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