Sandbox Reserved 1164

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== Structural highlights ==
== Structural highlights ==
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Structurally, the N-terminal extracellular domain () and the 7TM comprise the signature seven helical structure that is involved in the signaling via coupling to heterotrimeric proteins that activate adenylate cyclase to increase the levels of intracellular cyclic AMP, and also heterotrimeric G proteins that increase inositol phosphate and intracellular calcium levels.
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Structurally, the N-terminal extracellular domain (<scene name='72/721535/Ecd/2'>ECD</scene>) and the 7TM comprise the signature seven helical structure that is involved in the signaling via coupling to heterotrimeric proteins that activate adenylate cyclase to increase the levels of intracellular cyclic AMP, and also heterotrimeric G proteins that increase inositol phosphate and intracellular calcium levels.
[[Image:Lig.jpg|350 px|left|thumb|Amino Acid sequence of Glucagon]]
[[Image:Lig.jpg|350 px|left|thumb|Amino Acid sequence of Glucagon]]

Revision as of 12:45, 22 March 2016

This Sandbox is Reserved from Jan 11 through August 12, 2016 for use in the course CH462 Central Metabolism taught by R. Jeremy Johnson at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1160 through Sandbox Reserved 1184.
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Human Class B Glucagon G-Protein Coupled Receptor

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References

  1. 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
  2. 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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