Substrate dependent selective recruitment for the co-activators by the use of the structure dynamics of nuclear receptor
| Project/Area Number |
26291015
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Hiroshima University |
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Principal Investigator |
Tate Shin-ichi 広島大学, 理学(系)研究科(研究院), 教授 (20216998)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥15,860,000 (Direct Cost: ¥12,200,000、Indirect Cost: ¥3,660,000)
Fiscal Year 2016: ¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2015: ¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2014: ¥5,720,000 (Direct Cost: ¥4,400,000、Indirect Cost: ¥1,320,000)
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| Keywords | nuclear receptor / co-activator / transient structure / NMR / structure dynamics / time resolution FRET / 核内受容体 / 低存在率構造 / 天然変性領域 / FRET / 共役因子リクルート / 安定同位体標識 / PPARg / 異方性核スピン効果 |
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| Outline of Final Research Achievements |
We explored the mechanism of the substrate-dependent selective recruitment of the co-activator to PPARg, a type of nuclear receptor. We determined the solution structure of PPARg in the complex with agonist to demonstrate the relative orientation between H3 and H4 surrounding to the co-activator biding pocket was changed, which have been never found in the X-ray structures.
We analyzed the low-population structure of the fragments having the PPARg binding motifs, LxxLL, in SRC1, a co-activator. We revealed that two fragments had different low population structures at the site of LxxLL motif and the C-terminal parts following the binding motif. We also found the C-terminal low population structures are responsible for the co-activator binding to the PPARg. The dynamic structural properties of SRC1 should determine the substrate-dependent co-activator recruitment to the PPARg.
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Report
(4 results)
Research Products
(35 results)
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[Journal Article] Non-RVD mutations that enhance the dynamics of the TAL repeat array along the superhelical axis improve TALEN genome editing efficacy2016
Author(s)
Tochio,N., Umehara,K., Uewaki,J., Flechsig,H., Kondo,M., Dewa,T., Sakuma,T., Yamamoto,T., Saito,T., Togashi,T., Tate,S.
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Journal Title
Scientific Reports
Volume: 6
Issue: 1
Pages: 37887-37887
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Allosteric breakage to the hydrogen bond within the dual-histidine motif in the active site of human Pin1 PPIase2015
Author(s)
Wang,J., Tochio,N., Kawasaki,R., Tamari,Y., Xu,N., Uewaki,J., Utsunomiya-Tate,N., Tate,S.
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Journal Title
Biochemistry
Volume: 54
Issue: 33
Pages: 5242-5253
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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[Journal Article] Coating the outer surface of glass nanopipette with chlorobenzene-terminated polysilioxane2015
Author(s)
Takami,T., Ojiro,Y., Ogawa,S., Takaku,Y., Ogawa,Y., Saito,M., Matuoka,H., Tate,S.
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Journal Title
e-J.Surf.Sci. Nanotech
Volume: 13
Pages: 79-84
Related Report
Peer Reviewed
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[Journal Article] The C113D mutation in human Pin1 causes allosteric structural changes in the phosphate binding pocket of the PPIase domain through the tug of war in the dual-histidine motif2014
Author(s)
Xu,N., Tochio,N., Wang,J., Tamari,Y., Uewaki,J., Utsunomiya-Tate,N., Igarashi,K., Shiraki,T, Kobayashi,N., Tate,S.
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Journal Title
Biochemistry
Volume: 53
Issue: 34
Pages: 5568-5578
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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