Sandbox Reserved 1100: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Judith Weber (talk | contribs) No edit summary |
No edit summary |
||
| Line 18: | Line 18: | ||
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 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 <scene name='82/829353/7tm/1'>seven transmembrane helices</scene> linked thanks to three extracellular loops and three intracellular loops. The helix I | 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 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 <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 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 <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 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. | ||
| Line 39: | Line 39: | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
