Structural basis of polarity protein LGN in complex with its partner molecules
Project/Area Number |
21770116
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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 | Kyushu University |
Principal Investigator |
YUZAWA Satoru Kyushu University, 大学院・医学研究院, 学術研究員 (40515029)
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Project Period (FY) |
2009 – 2010
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Project Status |
Completed (Fiscal Year 2010)
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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)
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Keywords | 蛋白質 / シグナル伝達 / 分子認識 / X線結晶構造解析 / 細胞極性 |
Research Abstract |
A complex in which LGN associates with a partner molecule, Insc, plays a crucial role in regulating cell polarity. To elucidate the interaction between LGN and Insc based on its tertiary structure, we have been carried out structural studies of LGN-Insc compelx using by X-ray crystallography. Regions of LGN-Insc interaction as a construct suitable for structural studies were identified and then we established the preparation of the complex. We performed crystallization trials on the LGN-Insc complex and obtained crystals suitable for X-ray diffraction after optimization of crystallization condition. X-ray diffraction data were collected to a resolution of 2.8 Å for crystals of the LGN-Insc complex.
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Report
(3 results)
Research Products
(12 results)
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[Journal Article] The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site.2009
Author(s)
Bae, J-H., Lew, D.E., Yuzawa, S., Tome, F., Lax, I., Schlessinger, J.
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Journal Title
Related Report
Peer Reviewed
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[Journal Article] The domain organization of p67^<phox>, a protein required for activation of the superoxide-producing NADPH oxidase in phagocytes.2009
Author(s)
Yuzawa, S., Miyano, K., Honbou, K., Inagaki, F., Sumimoto, H.
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Journal Title
J.Innate Immun. 1
Pages: 543-555
Related Report
Peer Reviewed
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[Journal Article] The selectivity of receptor tyrosine kinasc signaling is controlled by a secondary SH2 domain binding site.2009
Author(s)
Bae, J-H., Lew, D.E. Yuzawa, S., Tome, F., Lax, I., Schlessinger, J.
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Journal Title
Related Report
Peer Reviewed
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[Presentation] The domain organization of p67^<phox>, a protein required for activation of the superoxide-producing NADPH oxidase in hagocytes2009
Author(s)
Yuzawa, S., Miyano, K., Honbou, K., Inagaki, F., Sumimoto, H.
Organizer
第32回 日本分子生物学会年会
Place of Presentation
横浜
Year and Date
2009-12-12
Related Report
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