Sandbox Reserved 1449: Difference between revisions
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MOR-1 is a G-protein coupled receptor (GPCRs), which binds extracellular signaling molecules including exogenous opiate drugs (such as morphine, codeine, and heroin) and endogenous opioid peptide neurotransmitters (such as enkephalins, endorphins, and dynorphins) as ligands to hinder pain-signaling. Endogenous opioids play a role in naturally reducing sensations of pain felt by the body. However, they do not evoke as powerful a physiological response as exogenous opioids. <ref>DOI: 10.1124/pr.112.007138</ref> | MOR-1 is a G-protein coupled receptor (GPCRs), which binds extracellular signaling molecules including exogenous opiate drugs (such as morphine, codeine, and heroin) and endogenous opioid peptide neurotransmitters (such as enkephalins, endorphins, and dynorphins) as ligands to hinder pain-signaling. Endogenous opioids play a role in naturally reducing sensations of pain felt by the body. However, they do not evoke as powerful a physiological response as exogenous opioids. <ref>DOI: 10.1124/pr.112.007138</ref> | ||
In the presence of a signaling molecule, an active G protein will have GTP bound to | In the presence of a signaling molecule, an active G protein will have GTP bound, to promote an intracellular signaling cascade. After the G protein has transduced the signal, it exchanges GTP for GDP and becomes inactive until another signaling molecule binds to the GPCR. | ||
In the case of the μ-opioid receptor, the binding of an opioid signaling molecule induces a conformational change in the receptor that activates an inhibitory G-protein (Gαi/o). This results in the dissociation of the G-protein complex. The Gα subunit then inhibits adenylyl cyclase. The Gβγ subunit acts to inhibit Ca2+ channels while activing K+ channels. While much has been learned about μ-opioid receptors since their discovery in 1973, there is still much that is unknown about their structure and activation mechanism. Thus, further research into this area is needed. <ref>DOI: 10.1016/j.str.2011.08.003</ref> | In the case of the μ-opioid receptor, the binding of an opioid signaling molecule induces a conformational change in the receptor that activates an inhibitory G-protein (Gαi/o). This results in the dissociation of the G-protein complex. The Gα subunit then inhibits adenylyl cyclase. The Gβγ subunit acts to inhibit Ca2+ channels while activing K+ channels. While much has been learned about μ-opioid receptors since their discovery in 1973, there is still much that is unknown about their structure and activation mechanism. Thus, further research into this area is needed. <ref>DOI: 10.1016/j.str.2011.08.003</ref> | ||
