pubmed-article:18162180 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18162180 | lifeskim:mentions | umls-concept:C0006864 | lld:lifeskim |
pubmed-article:18162180 | lifeskim:mentions | umls-concept:C0243192 | lld:lifeskim |
pubmed-article:18162180 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
pubmed-article:18162180 | lifeskim:mentions | umls-concept:C0378126 | lld:lifeskim |
pubmed-article:18162180 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
pubmed-article:18162180 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:18162180 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
pubmed-article:18162180 | lifeskim:mentions | umls-concept:C1710548 | lld:lifeskim |
pubmed-article:18162180 | pubmed:issue | 1-2 | lld:pubmed |
pubmed-article:18162180 | pubmed:dateCreated | 2008-2-4 | lld:pubmed |
pubmed-article:18162180 | pubmed:abstractText | Cannabinoid drugs differ in their rank order of potency to produce analgesia versus other central nervous system effects. We propose that these differences are due to unique agonist-bound cannabinoid CB1 receptor conformations that exhibit different affinities for individual subsets of intracellular signal transduction pathways. In order to test this hypothesis, we have used plasmon-waveguide resonance (PWR) spectroscopy, a sensitive method that can provide direct information about ligand-protein and protein-protein interactions, and can detect conformational changes in lipid-embedded proteins. A recombinant epitope-tagged human cannabinoid CB1 receptor was expressed in insect Sf9 cells, solubilized and purified using two-step affinity chromatography. The purified receptor was incorporated into a lipid bilayer on the surface of the PWR resonator. PWR spectroscopy demonstrated that cannabinoid agonists exhibit high affinity (KD=0.2+/-0.03 nM and 2+/-0.4 nM for CP 55,940 and WIN 55,212-2, respectively) for the purified epitope tagged hCB(1) receptor. Interestingly however, these structurally different cannabinoid agonists shifted the PWR spectra in opposite directions, indicating that CP 55,940 and WIN 55,212-2 binding leads to different hCB1 receptor conformations. Furthermore, PWR experiments also indicated that these CP 55,940-and WIN 55,212-bound hCB1 receptor conformations exhibit slightly different affinities to an inhibitory G protein heterotrimer, Gi1 (KD=27+/-8 nM and KD=10.7+/-4.7 nM, respectively), whereas they strikingly differ in their ability to activate this G protein type. | lld:pubmed |
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pubmed-article:18162180 | pubmed:language | eng | lld:pubmed |
pubmed-article:18162180 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18162180 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:18162180 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18162180 | pubmed:month | Feb | lld:pubmed |
pubmed-article:18162180 | pubmed:issn | 0014-2999 | lld:pubmed |
pubmed-article:18162180 | pubmed:author | pubmed-author:HrubyVictor... | lld:pubmed |
pubmed-article:18162180 | pubmed:author | pubmed-author:TollinGordonG | lld:pubmed |
pubmed-article:18162180 | pubmed:author | pubmed-author:DevanathanSav... | lld:pubmed |
pubmed-article:18162180 | pubmed:author | pubmed-author:StropovaDagma... | lld:pubmed |
pubmed-article:18162180 | pubmed:author | pubmed-author:RoeskeWilliam... | lld:pubmed |
pubmed-article:18162180 | pubmed:author | pubmed-author:YamamuraHenry... | lld:pubmed |
pubmed-article:18162180 | pubmed:author | pubmed-author:SalamonZdzisl... | lld:pubmed |
pubmed-article:18162180 | pubmed:author | pubmed-author:VargaEvaE | lld:pubmed |
pubmed-article:18162180 | pubmed:author | pubmed-author:GeorgievaTeod... | lld:pubmed |
pubmed-article:18162180 | pubmed:author | pubmed-author:ParkChad KCK | lld:pubmed |
pubmed-article:18162180 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18162180 | pubmed:day | 26 | lld:pubmed |
pubmed-article:18162180 | pubmed:volume | 581 | lld:pubmed |
pubmed-article:18162180 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18162180 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18162180 | pubmed:pagination | 19-29 | lld:pubmed |
pubmed-article:18162180 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
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pubmed-article:18162180 | pubmed:meshHeading | pubmed-meshheading:18162180... | lld:pubmed |
pubmed-article:18162180 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18162180 | pubmed:articleTitle | Unique agonist-bound cannabinoid CB1 receptor conformations indicate agonist specificity in signaling. | lld:pubmed |
pubmed-article:18162180 | pubmed:affiliation | Department of Medical Pharmacology, The University of Arizona, Tucson, Arizona, 85721, United States. | lld:pubmed |
pubmed-article:18162180 | pubmed:publicationType | Journal Article | lld:pubmed |
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