Sandbox Ben Whiteside: Difference between revisions
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<scene name='10/1038828/Ramp_ctr_interface/9'>RAMP CTR Interface </scene> is a key interaction that stabilizes the protein complex and positions the receptor to favorably bind to amylin. The RAMP-CTR interface extends into the plasma membrane, providing additional non-covalent bonding between the protein complex and the cell membrane. | <scene name='10/1038828/Ramp_ctr_interface/9'>RAMP CTR Interface </scene> is a key interaction that stabilizes the protein complex and positions the receptor to favorably bind to amylin. The RAMP-CTR interface extends into the plasma membrane, providing additional non-covalent bonding between the protein complex and the cell membrane. | ||
==== Extracellular Domain - RAMP interactions ==== | ==== Extracellular Domain - RAMP interactions ==== | ||
The extracellular domain of the CTR primarily contains polar residues in the extracellular space. In order to orient these residues | The extracellular domain of the CTR primarily contains polar residues in the extracellular space. In order to orient these residues to facilitate amylin binding, <scene name='10/1038828/Ctr_ramp_ecd_stablization/7'>RAMP makes hydrogen bonds with the CTR</scene> to increase the rigidity of the receptor binding site. | ||
== Clinical Significance == | == Clinical Significance == | ||
