2010 Fiscal Year Final Research Report
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 |
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| Research Field |
Structural biochemistry
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| Research Institution | Kyushu University |
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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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| 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 |
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| 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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Research Products
(6 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
Peer Reviewed
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