Orexin and Orexin receptor: Difference between revisions
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Michal Harel (talk | contribs) New page: <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> == Function == The '''orexin''' neuropeptides, <scene name='74/746099/Orexin-a/1'>O... |
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
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== Function == | == Function == | ||
The '''orexin''' neuropeptides, | The '''orexin''' neuropeptides, Orexin-A and Orexin-B, can excite neurons in the brain and affect multiple systems, including the acetylcholine, dopamine, histamine, and norepinephrine systems <ref name="two">doi:10.4088/JCP.13011su1c </ref><ref>PMID:15479620</ref><ref>PMID:10583376</ref>. These orexin neuropeptides bind to two subtypes of '''orexin receptors''', [http://www.rcsb.org/pdb/explore/jmol.do?structureId=4ZJ8&residueNr=SUV Orexin receptor 1] and [http://www.rcsb.org/pdb/explore/jmol.do?structureId=4S0V&residueNr=SUV Orexin receptor 2], both of which are G protein coupled receptors (GPCRs) <ref>doi:10.1038/nsmb.3183</ref>. The GPCRs can sense a molecule outside the cell and send a signal through transduction in order to cause the cells to respond <ref>PMID:9491897 </ref>. Thus, binding of the two can control wakefulness in humans. In studies, Orexin-B has shown to be more selective in binding, choosing to bind to Orexin receptor type 2 a majority of the time. Orexin-A has shown an equal selectivity at both types of receptors <ref name="two" />. | ||
== Disease == | == Disease == | ||
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== Relevance == | == Relevance == | ||
[[Belsomra]] or Suvorexant is a dual orexin receptor antagonist, and has the ability to block both Orexin receptors 1 and 2, thus inhibiting the neuropeptides from binding. By blocking this interaction, sleep can occur <ref | [[Belsomra]] or Suvorexant is a dual orexin receptor antagonist, and has the ability to block both Orexin receptors 1 and 2, thus inhibiting the neuropeptides from binding. By blocking this interaction, sleep can occur <ref>PMID:27471419</ref>. | ||
== Structural highlights == | == Structural highlights == | ||
Revision as of 12:30, 3 January 2018
FunctionThe orexin neuropeptides, Orexin-A and Orexin-B, can excite neurons in the brain and affect multiple systems, including the acetylcholine, dopamine, histamine, and norepinephrine systems [1][2][3]. These orexin neuropeptides bind to two subtypes of orexin receptors, Orexin receptor 1 and Orexin receptor 2, both of which are G protein coupled receptors (GPCRs) [4]. The GPCRs can sense a molecule outside the cell and send a signal through transduction in order to cause the cells to respond [5]. Thus, binding of the two can control wakefulness in humans. In studies, Orexin-B has shown to be more selective in binding, choosing to bind to Orexin receptor type 2 a majority of the time. Orexin-A has shown an equal selectivity at both types of receptors [1]. DiseaseRelevanceBelsomra or Suvorexant is a dual orexin receptor antagonist, and has the ability to block both Orexin receptors 1 and 2, thus inhibiting the neuropeptides from binding. By blocking this interaction, sleep can occur [6]. Structural highlights |
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3D Structures of orexin and orexin receptor3D Structures of orexin and orexin receptor
Updated on 03-January-2018
ReferencesReferences
- ↑ 1.0 1.1 Krystal AD, Benca RM, Kilduff TS. Understanding the sleep-wake cycle: sleep, insomnia, and the orexin system. J Clin Psychiatry. 2013;74 Suppl 1:3-20. doi: 10.4088/JCP.13011su1c. PMID:24107804 doi:http://dx.doi.org/10.4088/JCP.13011su1c
- ↑ Kim HY, Hong E, Kim JI, Lee W. Solution structure of human orexin-A: regulator of appetite and wakefulness. J Biochem Mol Biol. 2004 Sep 30;37(5):565-73. PMID:15479620
- ↑ Lee JH, Bang E, Chae KJ, Kim JY, Lee DW, Lee W. Solution structure of a new hypothalamic neuropeptide, human hypocretin-2/orexin-B. Eur J Biochem. 1999 Dec;266(3):831-9. PMID:10583376
- ↑ Yin J, Babaoglu K, Brautigam CA, Clark L, Shao Z, Scheuermann TH, Harrell CM, Gotter AL, Roecker AJ, Winrow CJ, Renger JJ, Coleman PJ, Rosenbaum DM. Structure and ligand-binding mechanism of the human OX1 and OX2 orexin receptors. Nat Struct Mol Biol. 2016 Apr;23(4):293-9. doi: 10.1038/nsmb.3183. Epub 2016 Mar , 7. PMID:26950369 doi:http://dx.doi.org/10.1038/nsmb.3183
- ↑ Sakurai T, Amemiya A, Ishii M, Matsuzaki I, Chemelli RM, Tanaka H, Williams SC, Richardson JA, Kozlowski GP, Wilson S, Arch JR, Buckingham RE, Haynes AC, Carr SA, Annan RS, McNulty DE, Liu WS, Terrett JA, Elshourbagy NA, Bergsma DJ, Yanagisawa M. Orexins and orexin receptors: a family of hypothalamic neuropeptides and G protein-coupled receptors that regulate feeding behavior. Cell. 1998 Feb 20;92(4):573-85. PMID:9491897
- ↑ Norman JL, Anderson SL. Novel class of medications, orexin receptor antagonists, in the treatment of insomnia - critical appraisal of suvorexant. Nat Sci Sleep. 2016 Jul 14;8:239-47. doi: 10.2147/NSS.S76910. eCollection 2016. PMID:27471419 doi:http://dx.doi.org/10.2147/NSS.S76910