Belsomra: Difference between revisions

Belsomra adopts a conformation similar to that of a horseshoe when binding to either of the two orexin receptors. Through steric hindrance, this horseshoe conformation halts transmembrane domain movement by making contact with the alpha-helices of all transmembrane domains except for the first one upon entering the binding site of the receptor. <ref> doi: 10.1038/nature14035 </ref>. Types of interactions between Belsomra and both orexin receptor subtypes include Van Der Waals interactions, aromatic packing via the pi bonds of aromatic amino acids, and hydrogen bonding. The most significant hydrogen bond occurs between the amide of the orexin receptors’ Asn324 and a tertiary amide carbonyl on Belsomra. <ref> doi: 10.1038/nature14035 </ref>. Water molecules also play a role in hydrogen bonding via formation of bridges between the Belsomra drug itself and the orexin receptors’ Asn324 and His350. <ref> doi: 10.1038/nature14035 </ref>. Structural differences of the two orexin receptors’ binding sites involve only two amino acids: receptor 1 has a serine that is a threonine in receptor 2, and an alanine in receptor 1 is a threonine in receptor 2. <ref> doi: 10.1038/nature14035 </ref>.