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

Expression and Purification of Transmembrane domain of Syndecan-4 for NMR Structural Study

등록일
2008년 8월 12일 11시 52분 07초
접수번호
1301
발표코드
33P232포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅰ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
박태준, 이민혜, 김용애
한국외국어대학교 화학과, Korea
Syndecan-4 is a transmembrane heparan sulfate proteoglycan belonging to the syndecan family and they are present on most cell types. Syndecan-4 is known to bind to various molecules, such as basic fibroblast growth factor, midkine, and tissue factor pathway, via its heparan sulfate chain, and is thought to play many biological roles through its binding bio-mediators. To get better understand the mechanism and function of Syndecan-4, it is critical to elucidate the three-dimensional structure of it. Unfortunately, Syndecan-4 is membrane-bound protein that transverse the lipid bilayer of the cell membrane, so large-scale production of such integral membrane proteins has been limited by experimental adversities due to insufficient yields and low solubility of protein. And also it is hard to characterize the membrane-bound three-dimensional structure using conventional solution NMR and X-ray crystallography. In this study, we demonstrate the successful high level expression and purification of Syndecan-4 transmembrane domain to facilitate structural studies in complex with membrane environments by solid-state NMR spectroscopy. And we also present the solution NMR structural studies of Syndecan-4 in lipid micelle.

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