2010 Fiscal Year Final Research Report
Elucidation of dynamics and function of an iPS cell reprogramming factor Sox2 from the view point of an intrinsically disordered protein
Project/Area Number |
21770126
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Structural biochemistry
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Research Institution | 公益財団法人サントリー生命科学財団 (2010) Suntory Institute for Bioorganic Research (2009) |
Principal Investigator |
SUGASE Kenji 公益財団法人サントリー生命科学財団, 生物有機科学研究所, 主席研究員 (00300822)
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Project Period (FY) |
2009 – 2010
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Keywords | 分子認識及び相互作用 |
Research Abstract |
NMR relaxation dispersion studies revealed that Sox2 fluctuates when it is free in solution, in particular the N-terminal helix α1 and the regions contacting the helixα1 are unfolded with a population of 2%. In contrast, no relaxation dispersion was observed for Sox2 in the bound form, indicating that Sox is stable in the bound form on μs-ms timescales. Since the helix α1 binds directly to DNA, the fluctuation observed for the free form is supposed to be important for non-specific binding to DNA.
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Research Products
(12 results)
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[Journal Article] Calcitonin in a protochordate, Ciona intestinalis--the prototype of the vertebrate calcitonin/calcitonin gene-related peptide superfamily.2009
Author(s)
Sekiguchi T, Suzuki N, Fujiwara N, Aoyama M, Kawada T, Sugase K, Murata Y, Sasayama Y, Ogasawara M, Satake H
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Journal Title
FEBS J. Vol.276
Pages: 4437-4447
Peer Reviewed
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[Remarks] ホームページ等