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학술발표회초록보기

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  • 09월 12일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제110회 대한화학회 학술발표회, 총회 및 기기전시회 안내 The length of L2 loop is critical for caspase-7 active site conformation

등록일
2012년 8월 30일 16시 19분 43초
접수번호
1458
발표코드
BIO.P-762 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 17일 (수요일) 16:00~19:00
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
이영미, 강효진1, 정상전2
한국생명공학연구원 바이오나노연구단, Korea
1한국생명공학연구원 바이오나노연구센터, Korea
2한국생명공학연구원 바이오나노연구단, Korea
Caspase-7 serves as one of apoptotic executioners to cleave the majority of cellular substrates in apoptotic cells. The enzyme expressed as a proenzyme is activated by other caspases upon cell death signals. Crystal structures of caspase-7 revealed a large conformational difference of caspase-7 active site before and after activation, meaning that the activation accompanies a large conformational change of loops constituting the active site. In spite of extensive structural and biochemical analyses, however, a detailed molecular mechanism of the caspase activation remains to be solved. Here, we demonstrate that active sites conformation is close correlation between lengths of caspase-7 L2 loops into S2 subsite. We engineered caspase-7 mutagenesis series on L2 loops and crystallized procaspase-7 with its specific inhibitor, Ac-DEVD-CHO. The determined structure showed the first procaspase-7 bound to a specific caspase inhibitor, implying that the engineering itself gave caspase-7 a catalytic activity. Surprisingly, each heterodimeric structure showed different conformations corresponding to the precursor and matured caspase-7. Biochemical analysis with the mutants demonstrated that the length of L2 loop is pivotal for the enzyme activity.

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