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- W2005305764 abstract "The secondary structure of the human peripheral cannabinoid receptor CB2 was investigated according to chemical shift data obtained on lipid-reconstituted, functional CB2. The CB2 receptor, uniformly labeled with 13C and 15N, was produced by bacterial expression, purified in milligram quantities, and reconstituted in an agonist-bound form into unilamellar liposomes. One- and two-dimensional 13C and 15N spectra were recorded by solid-state magic-angle spinning (MAS) NMR. Homogeneity of the reconstitution was examined by measurement of the 31P chemical-shift anisotropy of the membrane phospholipids and functional integrity monitored by a G-protein activation assay. The acquired one- and two-dimensional 13C-, and 15N-MAS NMR spectra of CB2 were compared with Cα, Cβ, C=O, and N-H chemical shifts predicted from a computer model of CB2, obtained in microsecond time scale, all atom molecular dynamics simulations. Although experimental spectra suffered from heavy superposition of resonances, the comparison of theoretical and experimental spectra gave insights into secondary structure of protein domains. There is sufficient spectral resolution to partially assign the resonances of specifically labeled CB2. The prospects for spectroscopic targeting of structural changes that take place upon CB2 activation by a combination of NMR experiments and computer modeling will be discussed." @default.
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- W2005305764 date "2010-01-01" @default.
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- W2005305764 title "Secondary-Structure Analysis of Human Peripheral Cannabinoid Receptor CB2 Based on Solid-State 13C-,15N-MAS NMR and Molecular Dynamics Simulations" @default.
- W2005305764 doi "https://doi.org/10.1016/j.bpj.2009.12.3421" @default.
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