Belsomra: Difference between revisions

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== Structural Highlights ==

Belsomra assumes a conformation similar to that of a horseshoe when binding to either orexin receptor 1 or <scene name='74/746099/Suvorexant/4'>orexin receptor 2</scene>. 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 name="six"> 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’ <scene name='74/746099/Asn324_orx2/5'>Asn324</scene> and an amide on Belsomra. <ref name="six" />. Water molecules also play a role in hydrogen bonding via formation of bridges between the Belsomra drug itself and the orexin receptors’ Asn324 and <scene name='74/746099/His350/2'>His350</scene>. <ref name="six" />. 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 <scene name='74/746099/Thr135_orx2/1'>threonine in receptor 2</scene>. <ref name="six" />.

Belsomra assumes a conformation similar to that of a horseshoe when binding to either orexin receptor 1 or <scene name='74/746099/Suvorexant/4'>orexin receptor 2</scene>. 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 name="six"> 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’ <scene name='74/746099/Asn324_orx2/5'>Asn324</scene> and an amide on Belsomra. <ref name="six" />. Water molecules also play a role in hydrogen bonding via formation of bridges between the Belsomra drug itself and the orexin receptors’ Asn324 and <scene name='74/746099/His350/2'>His350</scene>. <ref name="six" />. 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 <scene name='74/746099/Ala127_orx1/1'>alanine in receptor 1</scene> is a <scene name='74/746099/Thr135_orx2/1'>threonine in receptor 2</scene>. <ref name="six" />.

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Revision as of 00:53, 8 December 2016 view source Lisa M Konort (talk \| contribs) 34 edits No edit summary ← Older edit		Revision as of 01:01, 8 December 2016 view source Lisa M Konort (talk \| contribs) 34 edits No edit summary Newer edit →
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	== Structural Highlights ==		== Structural Highlights ==
	Belsomra assumes a conformation similar to that of a horseshoe when binding to either orexin receptor 1 or <scene name='74/746099/Suvorexant/4'>orexin receptor 2</scene>. 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 name="six"> 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’ <scene name='74/746099/Asn324_orx2/5'>Asn324</scene> and an amide on Belsomra. <ref name="six" />. Water molecules also play a role in hydrogen bonding via formation of bridges between the Belsomra drug itself and the orexin receptors’ Asn324 and <scene name='74/746099/His350/2'>His350</scene>. <ref name="six" />. 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 <scene name='74/746099/Thr135_orx2/1'>threonine in receptor 2</scene>. <ref name="six" />.		Belsomra assumes a conformation similar to that of a horseshoe when binding to either orexin receptor 1 or <scene name='74/746099/Suvorexant/4'>orexin receptor 2</scene>. 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 name="six"> 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’ <scene name='74/746099/Asn324_orx2/5'>Asn324</scene> and an amide on Belsomra. <ref name="six" />. Water molecules also play a role in hydrogen bonding via formation of bridges between the Belsomra drug itself and the orexin receptors’ Asn324 and <scene name='74/746099/His350/2'>His350</scene>. <ref name="six" />. 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 <scene name='74/746099/Ala127_orx1/1'>alanine in receptor 1</scene> is a <scene name='74/746099/Thr135_orx2/1'>threonine in receptor 2</scene>. <ref name="six" />.