Sandbox Ben Whiteside: Difference between revisions
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==== Bypass Motif ==== | ==== Bypass Motif ==== | ||
[[Image:SCT_rAmy_Overlay_v2.png|200 px|left|thumb|Figure 1: Overlay of sCT (orange) without the bypass motif and rAmy containing the bypass motif (green).]] | [[Image:SCT_rAmy_Overlay_v2.png|200 px|left|thumb|Figure 1: Overlay of sCT (orange) without the bypass motif and rAmy containing the bypass motif (green).]] | ||
The <scene name='10/1038869/Bypass_overview/3'>Bypass Motif</scene> 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 <scene name='10/1038869/Sct_bypass/1'>Calcitonin</scene>. When RAMP binds the receptor, it is forced into a new, rigid conformation, which interferes with calcitonin binding. Amylin's bypass motif contains a backbone configuration that does not interfere with AMYR, allowing the C-terminus of the peptide to interact with the extracellular domain. The Bypass Motif also binds <scene name='10/1038869/Bypass-ecdl_h-bond/4'>extracellular domain loop 4</scene> and makes <scene name='10/1038869/Bypass-amyr/3'>hydrophobic interactions</scene> with the transmembrane region of AMYR, anchoring the peptide in place for the signaling process to occur. <ref name="Cao">PMID:35324283</ref> | The <scene name='10/1038869/Bypass_overview/3'>Bypass Motif</scene> 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 <scene name='10/1038869/Sct_bypass/1'>Calcitonin</scene>. When RAMP binds the receptor, it is forced into a new, rigid conformation, which interferes with calcitonin binding (Figure 1). Amylin's bypass motif contains a backbone configuration that does not interfere with AMYR, allowing the C-terminus of the peptide to interact with the extracellular domain. The Bypass Motif also binds <scene name='10/1038869/Bypass-ecdl_h-bond/4'>extracellular domain loop 4</scene> and makes <scene name='10/1038869/Bypass-amyr/3'>hydrophobic interactions</scene> with the transmembrane region of AMYR, anchoring the peptide in place for the signaling process to occur. <ref name="Cao">PMID:35324283</ref> | ||
==Amylin Receptor Binding== | ==Amylin Receptor Binding== | ||