Sandbox Reserved 1100

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Revision as of 17:19, 14 January 2020

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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You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

1 Function
2 Disease
3 Relevance
4 Structural highlights

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 white and brown adipose tissues but some studies manifest that it could 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 for 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 and carboxykinase1, involved in gluconeogenesis.

1oen

G protein-coupled receptor

Disease

Relevance

Structural highlights

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 (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).

References

↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

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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 ~~caption='color'~~> (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 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 helix 0 (residues 121 to 129), seven transmembrane helices (residues 134 to 364) and an external C-terminus domain (residues 365 to 375).

Sandbox Reserved 1100

From Proteopedia

Revision as of 17:19, 14 January 2020

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