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== Mu Opioid Receptor== | == Mu Opioid Receptor== | ||
<StructureSection load='4n6h' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='4n6h' size='340' side='right' caption='Caption for this structure' scene=''> | ||
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Opioid receptors are G-protein coupled receptors (GPCR), which bind endogenous opioid peptide neurotransmitters (such as enkephalins and endorphins) and exogenous synthetic opiate drugs (such as morphine, codeine, and heroin) as ligands to hinder pain-signaling in the brain, peripheral nerves, and digestive tract. μ-opioid receptors are one of the four major classes of opioid receptors, which also includes δ-opioid receptors, κ-opioid receptors, and nociceptin opioid receptors. The μ-opioid receptor MOR-1 is expressed by the gene OPRM1 in vertebrates. The molecular structure of MOR-1 was better understood after its cloning in 1993. According to the American Society for Pharmacology and Experimental Therapeutics, the amino acid sequence of MOR-1 is 60-70% homologous to the other classes of opioid receptors. The difference between MOR-1 and the other opioid receptor proteins lies in its extracellular N-terminus, intracellular C-terminus, and second and third extracellular loops. The μ-opioid receptor is a 7-multispanning integral membrane protein found in dorsal root ganglion cells and peripheral nerve cells in humans, with its binding site exposed to the extracellular surface. The transmembrane domain of MOR-1 will dimerize at TM5 and TM6 to form oligomers. MOR-1 has important implications as a target for pain relievers as well as a treatment for drug abuse. | Opioid receptors are G-protein coupled receptors (GPCR), which bind endogenous opioid peptide neurotransmitters (such as enkephalins and endorphins) and exogenous synthetic opiate drugs (such as morphine, codeine, and heroin) as ligands to hinder pain-signaling in the brain, peripheral nerves, and digestive tract. μ-opioid receptors are one of the four major classes of opioid receptors, which also includes δ-opioid receptors, κ-opioid receptors, and nociceptin opioid receptors. The μ-opioid receptor MOR-1 is expressed by the gene OPRM1 in vertebrates. The molecular structure of MOR-1 was better understood after its cloning in 1993. According to the American Society for Pharmacology and Experimental Therapeutics, the amino acid sequence of MOR-1 is 60-70% homologous to the other classes of opioid receptors. The difference between MOR-1 and the other opioid receptor proteins lies in its extracellular N-terminus, intracellular C-terminus, and second and third extracellular loops. The μ-opioid receptor is a 7-multispanning integral membrane protein found in dorsal root ganglion cells and peripheral nerve cells in humans, with its binding site exposed to the extracellular surface. The transmembrane domain of MOR-1 will dimerize at TM5 and TM6 to form oligomers. MOR-1 has important implications as a target for pain relievers as well as a treatment for drug abuse. | ||
[https://www.youtube.com/watch?v=T5IbBX56OWw Mu Opioid Receptor] | |||
== Function == | == Function == | ||
