Sandbox Ben Whiteside: Difference between revisions
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==Structure== | ==Structure== | ||
==== Transmembrane Domain ==== | ==== Transmembrane Domain ==== | ||
Within the transmembrane domain (TMD) of the CTR, hydrophobic R groups span the phospholipid bilayer, anchoring the protein into the cell membrane upon amylin binding to the receptor. The interior of the transmembrane domain contains the hydrophilic residues | Within the transmembrane domain (TMD) of the CTR, hydrophobic R groups span the phospholipid bilayer, anchoring the protein into the cell membrane upon amylin binding to the receptor. The interior of the transmembrane domain contains the hydrophilic residues necessary for ligand binding and transduction of the signal across the cell membrane. | ||
====N-Terminus Disulfide==== | ====N-Terminus Disulfide==== | ||
The amylin peptide contains a <scene name='10/1038819/N_term_disulfide/3'>covalent disulfide linkage</scene> 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). Notable interactions formed by this disulfide include hydrogen bonds between E294 of the transmembrane domain with K1 of amylin, and both R362 and W361 of the transmembrane domain forming a hydrogen bond with N3 of amylin. | The amylin peptide contains a <scene name='10/1038819/N_term_disulfide/3'>covalent disulfide linkage</scene> 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). Notable interactions formed by this disulfide include hydrogen bonds between E294 of the transmembrane domain with K1 of amylin, and both R362 and W361 of the transmembrane domain forming a hydrogen bond with N3 of amylin. | ||