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  • 08월 28일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Characterization of InsP6 -dependent interaction between Nopp140 to CK2

등록일
2008년 8월 9일 19시 06분 27초
접수번호
0431
발표코드
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발표시간
목 <발표Ⅰ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
이상엽, 이원규, 유연규
국민대학교 생명나노화학과, Korea
Protein kinase CK2 (CK2) is a multifunctional protein serine / threonine kinase that phosphorylates many different proteins involved cellular processes, such as signal transduction, cell division, and proliferation. Human nucleolar phosphoprotein p140 (Nopp140) negatively regulates CK2, and the inhibitory activity of Nopp140 is interfered by inositol hexakisphosphate (InsP6). To characterize the critical domain of Nopp140 for its inhibition of CK2 activity, we prepared various Nopp140 fragments, and examined their affinity to CK2 using GST pull-down assay, Enzyme-Linked Immuno Sorbent Assay (ELISA), and Surface Plasmon Resonance (SPR). The C-terminus regions (amino acids 353-704), which is consisted of repetitive basic residues, is responsible for the interaction with CK2. Also the inhibitory mechanism of InsP6 on the interaction between Nopp140 and CK2 was examined by determining the binding partner of InsP6. When the mixture of InsP6 and CK2 or Nopp140 was analyzed by size-exclusion chromatography, InsP6 was co-eluted along with CK2 indicating that InsP6 binds to CK2.

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