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- W2022209712 abstract "The cannabinoid CB2 receptor is a Class A GPCR that is highly expressed in the immune system (Galiegue et al., 1995) and couples via Gi proteins (Glass and Northup, 1999). In a project to determine the stoichiometry of the CB2/ Gi protein complex, we first performed crosslinking experiments using a homobifunctional Lys-Lys linker, disuccinimidyl suberate combined with MS/MS analysis. We identified the following crosslinks: (1) Gi: K349 / CB2: K6.35(245) and (2) Gi: K317 / CB2: K5.64 (215). Using HgCl2 (and verified via MS/MS analysis), we also found disulfide bridge formation between Gi: C351 / CB2: C3.53(134). A computer model of the CB2/G-protein complex was constructed using our CB2 inactive (R) and active (R∗) state models (Hurst et al., 2010), along with the crystal structure of Gαi1β1γ2 (Wall et al., 1995). Our modelling revealed that achieving all three crosslinks at the same time would require CB2 to be in a homodimeric form, with one monomer in the inactive state, while the second monomer is in the activated state, coupled to G protein. This arrangement is consistent with the homodimeric signalling unit proposed by Javitch and Weinstein (Han et al., 2009). Further, to satisfy all of the experimental restraints, the interface of the CB2 homodimer had to be at TMH5-TMH6. This interface is similar to that found for the chemokine CXCR4 receptor (Wu et al., 2010). Monomer crosslinking studies were then undertaken to identify the homodimer interface in CB2. Substituted cysteine experiments revealed that in the presence of HgCl2, CB2 can dimerize at H6.57(267)C and at A6.60(270)C. These results are in agreement with the dimer interface chosen above to satisfy all of the CB2/G-protein crosslinks. [Support: RO1 DA003934 and KO5 DA021358 (PHR)]." @default.
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- W2022209712 date "2012-01-01" @default.
- W2022209712 modified "2023-10-18" @default.
- W2022209712 title "Structure of a Cannabinoid Receptor Subtype 2 Homodimer Determined by Cysteine and Homobifunctional Crosslinking Experiments Combined with Computational Studies" @default.
- W2022209712 doi "https://doi.org/10.1016/j.bpj.2011.11.1344" @default.
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