User:Mathias Vander Eide/Sandbox 1
Human Amylin Receptor with Associated RAMP1Human Amylin Receptor with Associated RAMP1
Overall structure of the Amylin GPCR bound to Amylin ligand This is a default text for your page Mathias Vander Eide/Sandbox 1. Click above on edit this page to modify. Be careful with the < and > signs. 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. IntroductionFunctionDiseaseAlzheimer'sRelevanceWeight LossStructural ComponentsCalcitonin ReceptorRAMPPeptide
Bypass MotifThe is a series of residues in the midsection of the amylin peptide that are crucial for providing structural specificity for the AMYR. Without RAMP association, the CTR is in a relaxed, fluid state, allowing the binding of calcitonin. When RAMP binds the receptor, it is forced into a new, rigid conformation, which interferes with calcitonin binding. Amylin's bypass motif
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ReferencesReferences
- ↑ 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
Student ContributorsStudent Contributors
- Mathias Vander Eide
- Andrew Helmerich
- Ben Whiteside