Mitoxantrone binds to Nopp140, an intrinsically unstructured protein,and modulate its interaction with protein kinase CK2

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Title
Mitoxantrone binds to Nopp140, an intrinsically unstructured protein,and modulate its interaction with protein kinase CK2
Author(s)
W K Lee; S Y Lee; J H Na; S Jang; C R Park; S Y Kim; Si Hyoung Lee; Kyou Hoon Han; Y G Yu
Bibliographic Citation
Bulletin of Korean Chemical Society, vol. 33, no. 6, pp. 2005-2011
Publication Year
2012
Abstract
Nopp140 is a highly phosphorylated protein that resides in the nucleolus of mammalian cell and is involved in the biogenesis of the nucleolus. It interacts with a variety of proteins related to the synthesis and assembly of the ribosome. It also can bind to a ubiquitous protein kinase CK2 that mediates cell growth and prevents apoptosis. We found that Nopp140 is an intrinsically unfolded protein (IUP) lacking stable secondary structures over its entire sequence of 709 residues. We discovered that mitoxantrone, an anticancer agent, was able to enhance the interaction between Nopp140 and CK2 and maintain suppressed activity of CK2. Surface plasma resonance studies on different domains of Nopp140 show that the C-terminal region of Nopp140 is responsible for binding with mitoxantrone. Our results present an interesting example where a small chemical compound binds to an intrinsically unfolded protein (IUP) and enhances protein-protein interactions.
Keyword
CK2Inositol-hexakisphosphateIntrinsically unfolded proteinMitoxantroneNopp140
ISSN
0253-2964
Publisher
Wiley
DOI
http://dx.doi.org/10.5012/bkcs.2012.33.6.2005
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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