Sandbox Ben Whiteside: Difference between revisions
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Within the transmembrane domain of the CTR, hydrophobic R groups span the phospholipid bilayer, anchoring the protein into the cell membrane upon amylin binding to the receptor. | Within the transmembrane domain of the CTR, hydrophobic R groups span the phospholipid bilayer, anchoring the protein into the cell membrane upon amylin binding to the receptor. | ||
===Chemical Modifications to Amylin=== | ===Chemical Modifications to Amylin=== | ||
====N | ====N-Terminus Disulfide==== | ||
The amylin peptide contains a covalent disulfide linkage between residues C2 and C7. This disulfide provides stability and rigidity to the helical structure of the peptide, allowing for favorable binding to the extracellular domain (ECD). | |||
====Amidated C-Terminus==== | |||
The C-terminus of amylin contains an amide group, rather than the traditional carboxylic acid group. This chemical modification allows for more extensive hydrogen bonding to nearby residues, due to the added hydrogen bond donor on the NH2 group. In turn, this allows for favorable hydrogen bonds between S129 of the transmembrane domain and the main chain of Y37 of amylin. This interaction causes a "kink" in the random coil of amylin, displacing Y37 into a hydrophobic pocket, allowing for favorable hydrophobic interactions with W79 of the transmembrane domain. | |||
=== Receptor Activity Modifying Proteins === | === Receptor Activity Modifying Proteins === | ||
<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. | ||
