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  • 08월 28일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Production and solid-state NMR structural studies of the second transmembrane domain from human wild-type & mutant melanocortin-4 receptor

2008년 8월 12일 11시 50분 12초
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목 <발표Ⅰ>
저자 및
최성섭, 박태준, 강가애, 김용애
한국외국어대학교 화학과, Korea
The melanocortin receptor family belongs to the superfamily of G protein-coupled receptors (GPCRs) which activate the adenylate cyclase signal transduction pathway. Recently, it has been suggested that normal melanocortin-4 receptor among five subtypes (MC1R-MC5R) increases energy expenditure and decreases food intake, and genetic disruption of MC4R cause obesity. Therefore, MC4 receptors may be ideal pharmacological targets for treating disorders such as obesity and anorexia. MC4R is membrane-bound protein that transverse the lipid bilayers of the cell membrane, so it is hard to express and characterize the membrane-bound three-dimensional structure by using conventional solution NMR and X-ray crystallography. In this study, to get better understand the structure-activity relationship between wild-type TM2 and D90N mutant TM2 peptides of MC4R, we cloned, expressed and purified both peptides. The yield was about 250mg/1L growth with a fusion partner. Here, we present the system that how can we obtained easily milligram quantities of pure, isotopically labeled peptide. The two recombinant peptides were characterized by tris-tricine polyacrylamide gel electrophoresis and their initial structural data was obtained and compared by solution NMR spectroscopy in the membrane-like environments. And we will also present solid-state NMR structural studies of aligned samples of transmembrane peptides.