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Structure and drug specificity of the human PTP family proteins

등록일
2006년 2월 24일 14시 32분 09초
접수번호
1233
발표코드
금17D3심 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 14시 : 30분
발표형식
심포지엄
발표분야
생명화학 - 생명2. Structural Genomics
저자 및
공동저자
류성언
생명공학연구원,
The human genome contains about 110 Protein tyrosine phosphatases (PTP) members that regulate cell growth/death, differentiation, immune system and brain functions. Consistent with their central roles in cellular functions, many PTPs are implicated in human diseases including cancer, diabetes and neuronal diseases. Despite the increasing efforts to develop therapeutic drugs targeting PTPs, the promising drug development has been hampered by the lack of detailed knowledge on the specificity and regulation of each enzyme. Recently, we determined crystal structures of eleven novel human PTPs. From the structures, we found that the active site of each PTP has significant diversity, suggesting the potential of specific inhibitor design targeting each enzyme. We are carrying out structure-based inhibitor screening of the PTPs by using chemical libraries. The structures also provide new insight into the mechanism of biological regulation for each enzyme.

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