期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 19, 期 2, 页码 -出版社
MDPI
DOI: 10.3390/ijms19020381
关键词
intrinsically disordered protein (IDP); nucleolar phosphoprotein 140 (Nopp140); conformational study; casein kinase 2 (CK2)
资金
- National Research Foundation of Korea (NRF) - Ministry of Science, ICT and Future Planning [2017M3A9C8060552, 2017M3A9C8060560]
- National Research Foundation of Korea [2016R1A2B4009952]
- National Research Foundation of Korea [2016R1A2B4009952, 2017M3A9C8060552, 2017M3A9C8060560] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Intrinsically disordered proteins (IDPs) represent approximately 30% of the human genome and play key roles in cell proliferation and cellular signaling by modulating the function of target proteins via protein-protein interactions. In addition, IDPs are involved in various human disorders, such as cancer, neurodegenerative diseases, and amyloidosis. To understand the underlying molecular mechanism of IDPs, it is important to study their structural features during their interactions with target proteins. However, conventional biochemical and biophysical methods for analyzing proteins, such as X-ray crystallography, have difficulty in characterizing the features of IDPs because they lack an ordered three-dimensional structure. Here, we present biochemical and biophysical studies on nucleolar phosphoprotein 140 (Nopp140), which mostly consists of disordered regions, during its interaction with casein kinase 2 (CK2), which plays a central role in cell growth. Surface plasmon resonance and electron paramagnetic resonance studies were performed to characterize the interaction between Nopp140 and CK2. A single-molecule fluorescence resonance energy transfer study revealed conformational change in Nopp140 during its interaction with CK2. These studies on Nopp140 can provide a good model system for understanding the molecular function of IDPs.
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