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 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 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- | 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> 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 <scene name='82/829353/7tm/1'>seven transmembrane helices</scene> 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. | ||
Concerning the extracellular faces, the three extracellular loops which connect the transmembrane helices are exposed and it is the same for the C-terminus domain. Besides, helices III and IV are longer than the other helices and as a result the C-terminal two turns of the helix VII 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 C-terminus domain. Besides, helices III and IV are longer than the other helices and as a result the C-terminal two turns of the helix VII protrude and are exposed too. | ||
The seven transmembrane helices surround a large internal cavity where a zinc-binding site 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 helices V and VI, and between the helices IV and VI. 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 zinc-binding site 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 helices V and VI, and between the helices IV and VI. It has been assumed that these openings are involved in the entrance and exit of both substrate and product. | ||
