Structural study of the chromosomal crossing-over resolution by the progeroid syndrome helicases
Project/Area Number |
21770113
|
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 | Nara Institute of Science and Technology |
Principal Investigator |
KITANO Ken 奈良先端科学技術大学院大学, バイオサイエンス研究科, 助教 (40346309)
|
Project Period (FY) |
2009 – 2010
|
Project Status |
Completed (Fiscal Year 2010)
|
Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2010: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2009: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
|
Keywords | タンパク質 / X線結晶構造解析 / ヘリカーゼ / ウェルナー症候群 / ブルーム症候群 / 三量体G タンパク質 / 阻害剤 / X線結晶構造解析 / RQCドメイン / HRDCドメイン / 三量体Gタンパク質 / X線 / 結晶構造解析 / ゲノム / 老化 |
Research Abstract |
Structural studies of the proteins that are associated with human accelerated-aging diseases and the proteins that function in the cell signaling pathway, have been performed. Three-dimensional structures of the “RQC domain of Werner syndrome WRN helicase in complex with double-stranded DNA”, “HRDC domain of Bloom syndrome BLM helicase”, and the “heterotrimeric G protein in complex with its specific inhibitor YM-254890” have been determined. These new structures offered insights into the field of biology and medicine.
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Report
(3 results)
Research Products
(32 results)
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[Journal Article] Solution structure of the HRDC domain of human Bloom syndrome protein BLM.2010
Author(s)
Sato, A., Mishima, M., Nagai, A., Kim, SY., Ito, Y., Hakoshima, T., Jee, JG., Kitano, K.
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Journal Title
J. Biochem.
Volume: 148(4)
Pages: 517-525
NAID
Related Report
Peer Reviewed
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[Journal Article] Structural basis for the specific inhibition of heterotrimeric G_q protein by a small molecule.2010
Author(s)
Nishimura, A.*, Kitano, K.*, Takasaki, J., Taniguchi, M., Mizuno, N., Tago, K., Hakoshima, T., Itoh, H. (*Both authors equally contributed)
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Journal Title
Proc. Natl. Acad. Sci. U.S.A.
Volume: 107(31)
Pages: 13666-13671
Related Report
Peer Reviewed
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[Journal Article] The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module.2010
Author(s)
Terawaki, S., Kitano, K., Mori, T., Zhai, Y., Higuchi, Y., Itoh, N., Watanabe, T., Kaibuchi, K., Hakoshima, T.
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Journal Title
EMBO J.
Volume: 29(1)
Pages: 236-250
Related Report
Peer Reviewed
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