Sandbox Reserved 1100: Difference between revisions

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== STRUCTURE ==

The Adiponectin receptor 1 is an integral membrane protein composed of 375 amino acids and its molecular weight is 42,4 kDa. This protein contains an internal <scene name='82/829353/N-terminus_domain/1'>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='82/829353/7tm/1'>seven transmembrane helices</scene> (residues 134 to 364) and an external <scene name='82/829353/C-terminus_domain/1'>C-terminus domain</scene> (residues 365 to 375).

The Adiponectin receptor 1 is an integral membrane protein composed of 375 amino acids and its molecular weight is 42,4 kDa. This protein contains 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='82/829353/7tm/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).

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/1'>N-terminus domain</scene> and an external <scene name='82/829353/C-terminus_domain/1'>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/Helix1/1'>helix I</scene> is formed by the residues 135 to 157, <scene name='82/829353/Helix2/1'>helix II</scene> by the residues 169 to 192, the <scene name='82/829353/Helix3/1'>helix III</scene> by the residues 198 to 227, the <scene name='82/829353/Helix4/1'>helix IV</scene> by the residues 232 to 252, the <scene name='82/829353/Helice5/1'>helix V</scene> by the residues 264 to 288 <scene name='82/829353/Helix6/1'>heliX VI</scene> by the residues 305 to 319 and the <scene name='82/829353/Helix7/1'>helix VII</scene> by the residues 336 to 364 .Besides, the <scene name='82/829353/Helix3/1'>helix III</scene> and <scene name='82/829353/Helix6/1'>heliX VI</scene> are longer than the other helices. These <scene name='82/829353/7tm/1'>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/1'>C-terminus domain</scene>. Besides, <scene name='82/829353/Helix3/1'>helix III</scene> and the <scene name='82/829353/Helix6/1'>heliX VI</scene>are longer than the other helices and as a result the <scene name='82/829353/C-terminus_domain/1'>C-terminus domain</scene> two turns of the ??? protrude and are exposed too.

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 == STRUCTURE ==
-The Adiponectin receptor 1 is an integral membrane protein composed of 375 amino acids and its molecular weight is 42,4 kDa. This protein contains an internal <scene name='82/829353/N-terminus_domain/1'>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='82/829353/7tm/1'>seven transmembrane helices</scene> (residues 134 to 364) and an external <scene name='82/829353/C-terminus_domain/1'>C-terminus domain</scene> (residues 365 to 375).
+The Adiponectin receptor 1 is an integral membrane protein composed of 375 amino acids and its molecular weight is 42,4 kDa. This protein contains 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='82/829353/7tm/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).
-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/1'>N-terminus domain</scene> and an external <scene name='82/829353/C-terminus_domain/1'>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/Helix1/1'>helix I</scene> is formed by the residues 135 to 157, <scene name='82/829353/Helix2/1'>helix II</scene> by the residues 169 to 192, the <scene name='82/829353/Helix3/1'>helix III</scene> by the residues 198 to 227, the <scene name='82/829353/Helix4/1'>helix IV</scene> by the residues 232 to 252, the <scene name='82/829353/Helice5/1'>helix V</scene> by the residues 264 to 288 <scene name='82/829353/Helix6/1'>heliX VI</scene> by the residues 305 to 319 and the <scene name='82/829353/Helix7/1'>helix VII</scene> by the residues 336 to 364 .Besides, the <scene name='82/829353/Helix3/1'>helix III</scene> and <scene name='82/829353/Helix6/1'>heliX VI</scene> are longer than the other helices. These <scene name='82/829353/7tm/1'>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/1'>C-terminus domain</scene>. Besides, <scene name='82/829353/Helix3/1'>helix III</scene> and the <scene name='82/829353/Helix6/1'>heliX VI</scene>are longer than the other helices and as a result the <scene name='82/829353/C-terminus_domain/1'>C-terminus domain</scene>  two turns of the ??? protrude and are exposed too.