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  • 02월 26일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제115회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Structural Studies of IP3 receptor: Toward understanding the regulatory mechanism

등록일
2015년 2월 25일 11시 11분 13초
접수번호
1326
발표코드
BIO.O-1 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 10시 : 00분
발표형식
구두발표
발표분야
생명화학 - Oral Presentation of Young Biochemists
저자 및
공동저자
서민덕
아주대학교 약학대학 약학과, 분자생물학괴, Korea

Inositol 1,4,5-trisphosphate receptors (IP3R) is an IP3-gated Ca2+ release channel on the ER membrane, and plays a critical role in controlling the cytosolic Ca2+ level of eukaryotic cells. The N-terminal region of IP3R is responsible for binding to IP3 and Ca2+ binding proteins such as Calcium-binding protein 1 (CaBP1) and calmodulin (CaM). In order to elucidate the structural basis for the regulatory mechanism of IP3R, X-ray crystallography and Nuclear Magnetic Resonance (NMR) were employed. Here, we present crystal structures of the N-terminal region (NT) of IP3R1 with (3.6 ?) and without (3.0 ?) IP3 bound. We also employed NMR to investigate the structure of the IP3R:CaBP1 complex in order to understand the regulatory mechanism of IP3R by CaBP1. We used the chemical shift perturbation (CSP) and paramagnetic relaxation enhancement (PRE) data to dock the structure of CaBP1 C-lobe onto the structure of IP3R?NT. The information acquired from these studies would contribute to design new therapeutic treatment for human diseases such as cardiovascular diseases and some kinds of cancers.


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