Elucidation of structure and function of mitochondrial voltage-dependent anion channel using the interacting molecules
Project/Area Number |
17K08296
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Biological pharmacy
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Research Institution | Institute of Physical and Chemical Research |
Principal Investigator |
Kimura-Someya Tomomi 国立研究開発法人理化学研究所, 生命機能科学研究センター, 上級研究員 (80450401)
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Project Period (FY) |
2017-04-01 – 2021-03-31
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Project Status |
Completed (Fiscal Year 2020)
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Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2019: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2018: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2017: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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Keywords | 無細胞タンパク質合成 / イオンチャネル / 大腸菌無細胞タンパク質合成 / チャネル / 相互作用化合物 / 蛋白質 / 薬学 / 生体分子 |
Outline of Final Research Achievements |
Voltage-dependent anion channel 1 (VDAC1), which is located in the outer mitochondrial membrane, plays important roles in various cellular processes. We determined high-resolution crystal structures of heptameric human VDAC1 prepared by using a cell-free protein synthesis system, which avoided the need for denaturation and refolding of the protein. We also tried to determine the structure of VDAC1 complexed with the interacting compound.
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Academic Significance and Societal Importance of the Research Achievements |
正しく折りたたまれたVDACの構造は、生体内での構造を反映していると考えられた。この構造に基づき、VDACに作用する化合物を設計したり、既存の相互作用化合物の最適化を行ったりすることで、VDACの関与が指摘されている疾患である、がんや神経変性疾患に対する治療薬の開発に繋がると考えられる。
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Report
(5 results)
Research Products
(17 results)
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[Journal Article] Metastable asymmetrical structure of shaftless V1 motor2019
Author(s)
S. Maruyama, K. Suzuki, M. Imamura, H. Sasaki, H. Matsunami, K. Mizutani, Y. Saito, F. L. Imai, Y. Ishizuka-Katsura, T. Kimura-Someya, M. Shirouzu, T. Uchihashi, T. Ando, I. Yamato, T. Murata
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Journal Title
Sci. Adv.
Volume: 5
Issue: 1
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Interhelical interactions between D92 and C218 in the cytoplasmic domain regulate proton uptake upon N-decay in the proton transport of Acetabularia rhodopsin II2018
Author(s)
Tamogami Jun, Kikukawa Takashi, Ohkawa Keisuke, Ohsawa Noboru, Nara Toshifumi, Demura Makoto, Miyauchi Seiji, Kimura-Someya Tomomi, Shirouzu Mikako, Yokoyama Shigeyuki, Shimono Kazumi, Kamo Naoki
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Journal Title
Journal of Photochemistry and Photobiology B: Biology
Volume: 183
Pages: 35-45
DOI
Related Report
Peer Reviewed
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