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제124회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Zinc fingers and its structural feature to generate specific interactions with their binding partners

2019년 8월 28일 13시 49분 56초
INOR.P-104 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 17일 (목요일) 11:00~12:30
Inorganic Chemistry
저자 및
Ka Young Son, Seung Jae Lee*
Department of Chemistry and Institute for Molecular Biology and Genetics, Chonbuk National University, Korea
Zinc finger proteins are one of 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 play critical roles in physiological systems from prokaryotes to eukaryotes. This presentation provides the structural details of several zinc finger proteins that are present in species ranging from prokaryotes to eukaryotes. The structural comparison of these zinc finger domains provides valuable information to the general authors of Journal of Microbiology and Biotechnology. These zinc fingers play pivotal roles because they generate transcriptional and translational activation and suppression against exogenous signals. Classical zinc finger proteins in physiological system play structural roles because they generate a specific fold, the ββα secondary structure, to recognize specific nucleic acids, proteins, lipids, and small molecules. Authors have explained the structural and functional details of zinc finger domains from basic aspects to specific changes. ZIF268, TFIIIA, GAGA, and Ros belong to the classical zinc finger family.