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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국자기공명학회 Journal of the Korean Magnetic Resonance Society Journal of the Korean Magnetic Resonance Society 제21권 제2호
- 발행연도
- 2017.1
- 수록면
- 72 - 77 (6page)
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β-catenin is a key signaling protein which regulates cell signaling and gene transcription. Abnormal activation of β-catenin is linked to many cancers, particularly with colorectal cancers. Although many genetic and biological studies on Wnt/β-catenin have been reported and structures of the complex between β-catenin and its diverse binding partners have been published, many of them have focused on armadillo repeat domain of β-catenin. Both N- and C-terminal domains have been suggested to regulate interactions of β-catenin with other molecules, but still little is known about the C-terminal unstructured domain. To investigate the structure of this domain, construct of C-terminus was designed and structural studies were performed using size exclusion chromatography (SEC), circular dichroism (CD), fluorescence and nuclear magnetic resonance (NMR) spectroscopy. We observed that not only the purified full-length construct but the purified C-terminal construct also dimerizes in solution by SEC, suggesting that this domain involves in dimerization of β-catenin. CD and fluorescence data indicate its flexibility and structural formation in the presence of membrane environments.
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