Opioid receptor

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spinqualitylabelsall models Structure of κ-opioid receptor complex with opioid antagonist, citric acid, PEG and octadec-enoate derivative (PDB entry 4djh) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Opioid 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. The μ-opioid receptor binds morphine. For more details on μ-opioid receptor see Mu Opioid Receptor Bound to a Morphinan Antagonist Kratom μ Opioid Receptors Mu Opioid Receptor Antagonists 6dde μ-opioid receptor: G protein complex The κ-opioid receptor binds opium-type ligands. For details see Student Project 3 for UMass Chemistry 423 Spring 2015. The δ-opioid receptor binds enkephalins. For details see Delta opioid receptor. The Nociceptin/orphanin FQ opioid receptor binds the heptadecapeptide orphanin[2]. 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[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 highlights The has a [5]. . Water molecules are shown as red spheres.

3D structures of opioid receptor

Updated on 20-August-2023 {{#tree:id=OrganizedByTopic|openlevels=0|

• δ-opioid receptor

• • 4ej4 – mOpR + naltrindole - mouse
    
  • 6pt2 – hOpR + peptide antagonist - human
    
  • 6pt3 – hOpR + antagonist
    
  • 8f7s – hOpR + GI + deltorphin – Cryo EM
    

• κ-opioid receptor

• • 4djh – hOpR + opioid antagonist
    
  • 6vi4 – hOpR (mutant) + nanobody
    
  • 7yit – hOpR (mutant) + nanobody + cytochrome b562
    
  • 7y1f – hOpR + GI + nanobody + dynorphin peptide – Cryo EM
    
  • 8dzr – hOpR (mutant`) + GI + nanobody + gustucin peptide – Cryo EM
    
  • 8dzp, 8dzs – hOpR (mutant`) + GI + nanobody + ligand – Cryo EM
    

• Nociceptin/orphanin FQ opioid receptor

• • 4ea3 – hOpR + peptide mimetic
    
  • 8f7w, 8f7x – hOpR + GI + nanobody + nociceptin peptide – Cryo EM
    

• μ-opioid receptor

• • 8efq – hOpR + GI + DAMGO peptide – Cryo EM
    
  • 8f7r – hOpR + GI + nanobody + endomorphin peptide – Cryo EM
    
  • [[8f7rq] – hOpR + GI + nanobody + endorphin peptide – Cryo EM
    
  • 8ef6 – hOpR + GI + nanobody + morphin – Cryo EM
    
  • 7t2h, 7u2k, 8ef5, 8efb, 8efl, 8efo – hOpR + GI + nanobody + drug – Cryo EM
    
  • 4dkl, 5c1m – mOpR + opioid antagonist
    
  • 6ddf – mOpR + GI + DAMGO peptide – Cryo EM
    
  • 7u2l – mOpR + GI + nanobody – Cryo EM
    
  • 6dde – mOpR + GI + nanobody + DAMGO peptide – Cryo EM
    
  • 7t2g – mOpR + GI + antagonist – Cryo EM
    
  • 7scg – mOpR + GI + nanobody + antagonist – Cryo EM
    
  • 7ul4 – mOpR + megabody + drug – Cryo EM
    

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References

1. ↑ 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
2. ↑ 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
3. ↑ 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
4. ↑ 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
5. ↑ 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