Mechanism of signal transduction regulated by the interactions to cell membrane
| Project/Area Number |
16H04780
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Yokohama City University |
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Principal Investigator |
Kidera Akinori 横浜市立大学, 生命医科学研究科, 教授 (00186280)
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| Research Collaborator |
Moritsugu Kei
Huang Bo
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| Project Period (FY) |
2016-04-01 – 2019-03-31
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| Project Status |
Completed (Fiscal Year 2018)
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| Budget Amount *help |
¥16,900,000 (Direct Cost: ¥13,000,000、Indirect Cost: ¥3,900,000)
Fiscal Year 2018: ¥6,630,000 (Direct Cost: ¥5,100,000、Indirect Cost: ¥1,530,000)
Fiscal Year 2017: ¥6,630,000 (Direct Cost: ¥5,100,000、Indirect Cost: ¥1,530,000)
Fiscal Year 2016: ¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
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| Keywords | タンパク質 / シグナル伝達 / 分子シミュレーション / 蛋白質 |
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| Outline of Final Research Achievements |
Molecular mechanism of the signal transduction at the atomic level during the real time course is the problem to be solved in this study. We used the techniques of the molecular simulation. As the target system of the study is the guanine nucleotide exchange reaction occurring in Ras bound to SOS. Long molecular dynamics simulations of the SOS-Ras complex clarified that the key trigger to the domain motions in SOS is the binding of another Ras to the allosteric site located between the Rem domain and the Cdc25 domain in SOS. The resultant domain motions cause the significant motion of the helical hairpin near catalytic Ras, which in turn open up the switch 1 of Ras to release the bound GDP molecule. The relay of the motions is the molecular mechanism of the reaction, i.e., binding of allosteric Ras → domain motion of SOS → motion of helical hairpin → motion of switch 1 of Ras → the release of GDP.
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| Academic Significance and Societal Importance of the Research Achievements |
計算機の中に作り出した細胞環境を模擬した系の中で、刺激に対する応答として起こる一連の出来事のシミュレーションは、その結果の観察から実験ではとらえることができない実像としての生体分子が実時間で動く有様をとらえることができる。ここで得られた結果は、細胞における信号伝達の理解を物質のことばで解釈することを可能とし、さらには分子の振る舞いに対する細胞環境の役割を明らかにすることで、分子から細胞へと展開していくシミュレーションを用いた研究の方向を示すものと期待される。
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Report
(4 results)
Research Products
(19 results)
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[Journal Article] Structure of the Dnmt1 reader module complexed with a unique two-mono-ubiquitin mark on histone H3 reveals the basis for DNA methylation maintenance.2017
Author(s)
Ishiyama S, Nishiyama A, Saeki Y, Moritsugu K Morimoto D, Yamaguchi L, Arai N, Matsumura R, Kawakami T, Mishima Y, Hojo H, Shimamura S, Ishikawa F, Tajima S, Tanaka K, Ariyoshi M, Shirakawa M, Ikeguchi M, Kidera A, Suetake I, Arita K, Nakanishi M
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Journal Title
Mol Cell
Volume: 68
Issue: 2
Pages: 350-360
DOI
Related Report
Peer Reviewed / Open Access
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