Sandbox Reserved 1100

This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115.

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The AdipoR1 receptor

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D FUNCTION The protein adiponectin receptor 1 is one of the two receptors for the hormone called adiponectin. The adiponectin is an hormone, and more precisely an adipokine , present in the blood at high concentration, approximatively 0,01 % of the total amount of proteins in plasma.The human adiponectin monomer as molecular weight of about 28 kDa and is composed of 244 amino acids. However, the molecular weight of the hormone depends on the multimerization of this one . The hormone is mainly created by adipocytes present in brown and white adipose tissues but according to researches it could also be produced in some non-adipose tissues as in skeletal muscle .Two forms of adiponectin exist: the full-length adiponectin, presents in the liver and the globular adiponectin presents in skeletal muscles and in the liver.The adiponectin receptor 1 is a receptor sensitive in particular to the globular form. This hormone is known to be anti-diabetic, antiatherogenic and a regulator of tissue inflammation and insulin sensitivity. These properties of the adiponectin are linked to the fatty oxidation trigger by the hormone and the adipoR1 receptor. Different fatty acid oxidation pathway exists. The major pathway regulated by adipoR1 is the AMP kinase channel, but this pathway is not completely known. However, several studies show that adipoR1 decreases the hepatic glucose production by activating this channel. AdipoR1 is also able to limit the expression of enzymes, like glucose-6-phosphatase, phosphoenolpyruvate carboxykinase and carboxykinase1, involved in gluconeogenesis. 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 can be decomposed into different parts: an internal N-terminus domain (residues 89 to 120), a short intracellular domain called helix 0 (residues 121 to 129), seven transmembrane helices (residues 134 to 364) and an external C-terminus domain (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 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. Indeed in living cell both monomers and oligomers are present. A specific motif was identified to contribute to the AdipoR1 dimerization: it is the motif GxxxG in the transmembrane helix V. Besides, the dimerization of AdipoR1 is also regulated. This dimerization is inhibited by the fixation of the full-length adiponectin while the globular adiponectin has any impact on the dimerization level of the AdipoR1 receptor. Thanks to mutant experiment, it can be supposed that the collagen-like domain of the full-length adiponectin is responsible to the dimer dissociation. There are strong evidences that dimerization of the AdipoR1 receptor has a role during the biosynthesis, the trafficking and the signalling of the seven transmembrane receptors.