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  • 02월 22일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

High-level Expression and Purification of the Second Transmembrane Domain of Wild-type and Mutant Human Melanocortin-4 Receptor for Solid-State NMR

등록일
2008년 2월 14일 12시 32분 35초
접수번호
1359
발표코드
29P85포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 <발표Ⅴ>
발표형식
포스터
발표분야
물리화학
저자 및
공동저자
박태준, 최성섭, 강가애, 김용애
한국외국어대학교 화학과,
The melanocortin receptor family belongs to the superfamilly 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) decreases food intake, and genetic disruption of MC4R causes obesity. Therefore, MC4R may be ideal pharmacological targets for treating disorders such as obesity and anorexia. MC4R is membrane-bound protein that transverse 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, we expressed and purified the wild-type TM2 and mutant TM2 peptides of MC4R. We successfully cloned and optimized the expression condition and purified the MC4R wild-type TM2 and mutant TM2 peptide. The yield was 200mg/1L growth with a fusion partner KSI. The integrity of TM2 peptides was identified by NMR spectroscopy in the membrane-like environments.

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