期刊
JOURNAL OF PEPTIDE RESEARCH
卷 60, 期 3, 页码 169-177出版社
WILEY
DOI: 10.1034/j.1399-3011.2002.21012.x
关键词
cannabinoid receptor; CB2; circular dichroism; fourth cytoplasmic loop; helix 8; NMR
资金
- NIDA NIH HHS [DA11510] Funding Source: Medline
The cytoplasmic helix domain (fourth cytoplasmic loop, helix 8) of numerous G protein-coupled receptors (GPCRs) such as rhodopsin and the beta-adrenergic receptor exhibit unique structural and functional characteristics. Computer models also predict this structure for the cannabinoid CB2 receptor, another member of the GPCR superfamily. In our study, a peptide corresponding to helix 8 of the CB2 receptor was synthesized chemically and its secondary structure determined by circular dichroism (CID) and H-1 NMR spectroscopy. NMR and CID revealed an alpha-helical structure in this region in both dodecylphosphocholine micelles and dimethylsulfoxide, in contrast to a random coil configuration found in aqueous solvent. This finding is in good agreement with other previous GPCR structural studies including X-ray crystallography. By combining our finding with other studies, we further hypothesize that the amphipathic nature of helix 8 can play a significant role in the function and regulation of CB receptors as well as other GPCRs in general.
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