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Opioid Receptor: Its structure and how it works
Author(s) -
Crowthers Kevin,
Melo Hiliana,
Chen Yixin,
LaGanke Nicole,
Rooney Colleen,
Clouse Cameron,
Cunningham Chris
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.lb68
Subject(s) - receptor , opium , etorphine , transmembrane domain , g protein coupled receptor , opioid receptor , extracellular , opioid , chemistry , papaver , microbiology and biotechnology , pharmacology , biology , biochemistry , (+) naloxone , botany , political science , law
The First and Second Opium Wars were two conflicts caused by the the reaction of China over the illegal exportation of the drug opium by the British government. Opium, also known as poppy tears, is a narcotic drug extracted from the plant Papaver somniferum. This drug causes a sensation of euphoria and pain relief by binding to opioid receptors that exist on cell membranes of neurons and the digestive tract. Opioid receptors (OR) are G‐protein‐coupled receptors (GPCRs) with three main variables, μ‐OR, δ‐OR and κ‐OR. The μ‐OR is the most important opioid receptor for the management of pain. To better understand this receptor's structure and how it can impact function, the Worcester Academy SMART Team has modeled the μ‐OR using 3D printing technology. Using the irreversible antagonist β‐FNA, the μ‐OR has a complex shape, consisting of seven transmembrane α‐helices connected by three extracellular loops and three intracellular loops; transmembrane helices 5 and 6 are involved in receptor dimerization. The binding pocket is relatively open which causes a greater exposure to the extracellular surface, providing evidence as to why potent opioids like buprenorphine and etorphine have a rapid dissociation. β‐FNA interacts with 14 residues, of which nine have more interaction with the ligand and are conserved in the δ‐OR and the κ‐OR. The μ‐OR contains 11 identical amino acid residues with the the other two ORs. The only differences are the positions E229, K303 and W318, which are Asp, Trp and Leu. Further understanding of opioid receptors and their structure can lead to a way of treating pain without side effects.