Sandbox Reserved 1100: Difference between revisions

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== STRUCTURE ==
== 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 N-terminus domain (residues 89 to 120) (couleur = blueviolet) , a short intracellular domain called helix 0 (residues 121 to 129) (couleur = crimson ), seven transmembrane helices (residues 134 to 364) and an external C-terminus domain (residues 365 to 375) (color = magenta)
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/Helice0/1'>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 organisation of the structure of the Adiponectin receptor 1 is the opposite G-protein family. Indeed, the Adiponectin receptor has an internal N-terminus domain and an external C-terminus domain 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 G-protein family. Indeed, the Adiponectin receptor has an internal N-terminus domain and an external C-terminus domain while the G-protein family has an internal N-terminus domain and an external C-terminus domain.
The Adiponectin receptor 1 contains seven transmembrane helices linked thanks to three extracellular loops and three intracellular loops. The helix I (color= deepskybleu) is formed by the residues 135 to 157, helix II (color=seagreen) by the residues 169 to 192, the helix III (color=fushia) by the residues 198 to 227, the helix IV (color=grey)by the residues 232 to 252, the helix V(color=orangered) by the residues 264 to 288 the helix VI(color=blue) by the residues 305 to 319 and the helix VII (color = coral)by the residues 336 to 364.Besides, the helices III and VI are longer than the other helices. These seven transmembrane helices have a clockwise circular specific organisation (from helix I to helix VII) and form a bundle.
The Adiponectin receptor 1 contains seven transmembrane helices linked thanks to three extracellular loops and three intracellular loops. The helix I (color= deepskybleu) is formed by the residues 135 to 157, helix II (color=seagreen) by the residues 169 to 192, the helix III (color=fushia) by the residues 198 to 227, the helix IV (color=grey)by the residues 232 to 252, the helix V(color=orangered) by the residues 264 to 288 the helix VI(color=blue) by the residues 305 to 319 and the helix VII (color = coral)by the residues 336 to 364.Besides, the helices III and VI are longer than the other helices. These seven transmembrane helices have a clockwise circular specific organisation (from helix I to helix VII) and form a bundle.
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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 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/Helice0/1'>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).
 




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