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Intrinsically disordered fold of a PIAS1-binding domain of CP2b

Title
Intrinsically disordered fold of a PIAS1-binding domain of CP2b
Author
김철근
Keywords
CP2; PIAS1; IDR; NMR
Issue Date
2014-06
Publisher
Korean Magnetic Resonance Society
Citation
Journal of the Korean Magnetic Resonance Society, 2014, 18(1), P.30-35
Abstract
The transcription factor CP2 regulates various biological systems at diverse tissues and cells. However, none of the four CP2 isoforms has been solved in structure yet. In particular, two different regions of the CP2b isoform have been characterized to interact with the PIAS1 in nucleus to regulate the -globin gene expression. Among them, in this study, the region encompassing residues 251-309 of CP2b was prepared as a recombinant protein and its solution structure was characterized by NMR spectroscopy. The results indicated that the CP2b(251-309) fold belongs to typical IDRs (intrinsically disordered regions), likely to facilitate promiscuous interactions with various target proteins. Unfortunately, however, its interaction with the N-terminal domain of PIAS1 (residues 1-70), which has been identified as one of the CP2b-binding sites, was not observed in the NMR-based titration experiments. Therefore, it could be postulated that the 251-309 region of CP2b would not contact with the PIAS1(1-70), but alternatively interact with another CP2b-binding region that encompasses residues 400-651 of PIAS1.
URI
http://koreascience.or.kr/article/ArticleFullRecord.jsp?cn=JGGMB2_2014_v18n1_30https://repository.hanyang.ac.kr/handle/20.500.11754/71249
ISSN
1226-6531
DOI
10.6564/JKMRS.2014.18.1.030
Appears in Collections:
COLLEGE OF NATURAL SCIENCES[S](자연과학대학) > LIFE SCIENCE(생명과학과) > Articles
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