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  • 02월 19일 10시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

대한화학회 제121회 학술발표회 및 총회 Structural analyses of zinc finger proteins for specific interaction

등록일
2018년 2월 1일 15시 57분 08초
접수번호
3489
발표코드
INOR.P-36 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
4월 19일 (목요일) 11:00~12:30
발표형식
포스터
발표분야
Inorganic Chemistry
저자 및
공동저자
Ha Ra Jang, Seung Jae Lee*
Department of Chemistry and Research Institute for Molecular Biology and Genetics, Chonbuk National University, Korea
Zinc finger proteins are among the most extensively applied metalloproteins in the field of biotechnology due to their unique structural and functional aspects as transcriptional and translational regulators. The classical zinc fingers are the largest family of zinc proteins and they provide critical roles in physiological systems from prokaryotes to eukaryotes. Two cysteine and two histidine residues (Cys2His2) coordinate to the zinc ion for the structural functions to generate a ββα fold, and this secondary structure supports specific interactions with their binding partners including DNA, RNA, lipids, proteins, and small molecules. In this presentation, the structural similarity and differences of well-known Cys2His2 type zinc fingers such as zinc interaction factor 268 (ZIF268), transcription factor IIIA (TFIIIA), GAGA, and Ros will be explained. These proteins perform their specific roles in species from archaea to eukaryotes and they show significant structural similarity; however, their aligned amino acids present low sequence homology. These zinc finger proteins have different numbers of domains for their structural roles to maintain biological progress through transcriptional regulations from exogenous stresses. The superimposed structures of these finger domains provide interesting details when these fingers were applied to specific gene binding and editing. The structural information in this study will aid in the selection of unique types of zinc finger applications in vivo and in vitro approaches because biophysical backgrounds including complex structures and binding affinities aid in the protein design area.

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