Opioid receptor: Difference between revisions
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<StructureSection load=' | <StructureSection load='' size='350' side='right' caption='Structure of κ-opioid receptor complex with opioid antagonist, citric acid, PEG and octadec-enoate derivative (PDB entry [[4djh]])' scene='55/553941/Cv/1' pspeed='8'> | ||
== Function == | |||
'''Opioid receptor''' (OpR) is a G protein-coupled receptor with opioids as ligands. OpR types are classified according to the ligands which bind to them. The '''μ-opioid receptor''' binds morphine | '''Opioid receptor''' (OpR) is a [[G protein-coupled receptor]] with [[opioids]] as ligands<ref>PMID:22204322</ref>. OpR types are classified according to the ligands which bind to them.<br /> | ||
* The '''μ-opioid receptor''' binds morphine. For more details on μ-opioid receptor see<br /> | |||
**[[Mu Opioid Receptor Bound to a Morphinan Antagonist]] | |||
**[[Kratom]] | |||
**[[μ Opioid Receptors]] | |||
**[[Mu Opioid Receptor]] | |||
**[[Antagonists]] | |||
**[[6dde]] μ-opioid receptor: G protein complex<br /> | |||
* The '''κ-opioid receptor''' binds opium-type ligands. For details see [[Student Project 3 for UMass Chemistry 423 Spring 2015]].<br /> | |||
* The '''δ-opioid receptor''' binds enkephalins. For details see [[Delta opioid receptor]]. | |||
* The '''Nociceptin/orphanin FQ opioid receptor''' binds the heptadecapeptide orphanin<ref>PMID:23395957</ref>. | |||
See also | |||
*[[Opioids]] | |||
*[[Opioid receptors]] | |||
*[[Treatments:Opioid drugs]] | |||
*[[Tutorial: The opioid receptor, a molecular switch]] | |||
*[[Transmembrane (cell surface) receptors]] | |||
== Relevance == | |||
Nociceptin/orphanin FQ opioid receptor plays a role in the regulation of reward and motivation of substance abuse and is a target of drug abuse medication<ref>PMID:21050175</ref>. Its agonists are useful in treatment of pain, anxiety, edema and more and its antagonists are useful in pain management, depression, dementia and Parkinson disease<ref>PMID:17266536</ref>. | |||
== Structural highlights == | |||
The <scene name='55/553941/Cv/6'>κ-opioid receptor</scene> has a <scene name='55/553941/Cv/7'>large binding pocket</scene><ref>PMID:22437504</ref>. <scene name='55/553941/Cv/8'>Active site</scene>. Water molecules are shown as red spheres. | |||
</StructureSection> | |||
==3D structures of opioid receptor== | ==3D structures of opioid receptor== | ||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
{{#tree:id=OrganizedByTopic|openlevels=0| | |||
*δ-opioid receptor | |||
**[[4ej4]] – mOpR + naltrindole - mouse <br /> | |||
**[[6pt2]] – hOpR + peptide antagonist - human <br /> | |||
**[[6pt3]] – hOpR + antagonist <br /> | |||
**[[8f7s]] – hOpR + GI + deltorphin – Cryo EM <br /> | |||
*κ-opioid receptor | |||
**[[4djh]] – hOpR + opioid antagonist<br /> | |||
**[[6vi4]] – hOpR (mutant) + nanobody<br /> | |||
**[[7yit]] – hOpR (mutant) + nanobody + cytochrome b562<br /> | |||
**[[7y1f]] – hOpR + GI + nanobody + dynorphin peptide – Cryo EM <br /> | |||
**[[8dzr]] – hOpR (mutant`) + GI + nanobody + gustucin peptide – Cryo EM <br /> | |||
**[[8dzp]], [[8dzs]] – hOpR (mutant`) + GI + nanobody + ligand – Cryo EM <br /> | |||
*Nociceptin/orphanin FQ opioid receptor | |||
**[[4ea3]] – hOpR + peptide mimetic <br /> | |||
**[[8f7w]], [[8f7x]] – hOpR + GI + nanobody + nociceptin peptide – Cryo EM <br /> | |||
*μ-opioid receptor | |||
**[[8efq]] – hOpR + GI + DAMGO peptide – Cryo EM <br /> | |||
**[[8f7r]] – hOpR + GI + nanobody + endomorphin peptide – Cryo EM <br /> | |||
**[[8f7q]] – hOpR + GI + nanobody + endorphin peptide – Cryo EM <br /> | |||
**[[8ef6]] – hOpR + GI + nanobody + morphin – Cryo EM <br /> | |||
**[[7t2h]], [[7u2k]], [[8ef5]], [[8efb]], [[8efl]], [[8efo]] – hOpR + GI + nanobody + drug – Cryo EM <br /> | |||
**[[4dkl]], [[5c1m]] – mOpR + opioid antagonist <br /> | |||
**[[6ddf]] – mOpR + GI + DAMGO peptide – Cryo EM <br /> | |||
**[[7u2l]] – mOpR + GI + nanobody – Cryo EM <br /> | |||
**[[6dde]] – mOpR + GI + nanobody + DAMGO peptide – Cryo EM <br /> | |||
**[[7t2g]] – mOpR + GI + antagonist – Cryo EM <br /> | |||
**[[7scg]] – mOpR + GI + nanobody + antagonist – Cryo EM <br /> | |||
**[[7ul4]] – mOpR + megabody + drug – Cryo EM <br /> | |||
}} | |||
[[ | == References == | ||
<references/> | |||
[[Category:Topic Page]] | |||
Latest revision as of 10:18, 20 August 2023
FunctionOpioid receptor (OpR) is a G protein-coupled receptor with opioids as ligands[1]. OpR types are classified according to the ligands which bind to them.
See also
RelevanceNociceptin/orphanin FQ opioid receptor plays a role in the regulation of reward and motivation of substance abuse and is a target of drug abuse medication[3]. Its agonists are useful in treatment of pain, anxiety, edema and more and its antagonists are useful in pain management, depression, dementia and Parkinson disease[4]. Structural highlightsThe has a [5]. . Water molecules are shown as red spheres.
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3D structures of opioid receptor3D structures of opioid receptor
Updated on 20-August-2023
ReferencesReferences
- ↑ Feng Y, He X, Yang Y, Chao D, Lazarus LH, Xia Y. Current research on opioid receptor function. Curr Drug Targets. 2012 Feb;13(2):230-46. PMID:22204322
- ↑ Donica CL, Awwad HO, Thakker DR, Standifer KM. Cellular mechanisms of nociceptin/orphanin FQ (N/OFQ) peptide (NOP) receptor regulation and heterologous regulation by N/OFQ. Mol Pharmacol. 2013 May;83(5):907-18. doi: 10.1124/mol.112.084632. Epub 2013 Feb , 8. PMID:23395957 doi:http://dx.doi.org/10.1124/mol.112.084632
- ↑ Zaveri NT. The nociceptin/orphanin FQ receptor (NOP) as a target for drug abuse medications. Curr Top Med Chem. 2011;11(9):1151-6. PMID:21050175
- ↑ Chiou LC, Liao YY, Fan PC, Kuo PH, Wang CH, Riemer C, Prinssen EP. Nociceptin/orphanin FQ peptide receptors: pharmacology and clinical implications. Curr Drug Targets. 2007 Jan;8(1):117-35. PMID:17266536
- ↑ Wu H, Wacker D, Mileni M, Katritch V, Han GW, Vardy E, Liu W, Thompson AA, Huang XP, Carroll FI, Mascarella SW, Westkaemper RB, Mosier PD, Roth BL, Cherezov V, Stevens RC. Structure of the human kappa-opioid receptor in complex with JDTic. Nature. 2012 Mar 21;485(7398):327-32. doi: 10.1038/nature10939. PMID:22437504 doi:10.1038/nature10939