User:Mathias Vander Eide/Sandbox 1

Human Amylin Receptor with Associated RAMP1

spinqualitylabelsall models Human AMYR1 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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 or to the article describing Jmol to the rescue. Structural Components Peptide Amylin Peptide Amidated C-Terminus of Amylin Ligand N-Terminus disulfide bond on Amylin Ligand Bypass Motif The Bypass Motif 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 Bypass Motif Calcitonin Overlay of sCT (orange) and rAmy (green) Bypass Motif interaction with ECDloop4 Bypass Motif interaction with AMYR This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Student Contributors

• Mathias Vander Eide
• Andrew Helmerich
• Ben Whiteside

Proteopedia Page Contributors and Editors (what is this?)

Mathias Vander Eide