| Project/Area Number |
15K06962
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Kyushu University (2016-2017)
The University of Tokyo (2015) |
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Principal Investigator |
CAAVEIRO Jose 九州大学, 薬学研究院, 准教授 (00536732)
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| Research Collaborator |
TSUMOTO Kouhei 東京大学, 大学院工学系研究科, 教授
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | Glycan / Sugar / Antibody / Enzyme / Pore-forming protein / X-ray crystallography / Thermodynamics / Kinetics / glycan / sugar / antibody / enzyme / pore forming protein / kinetics / Antobody / Pore forming protein / Thernodynamics / X-ray Crystallography |
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| Outline of Final Research Achievements |
We clarified the thermodynamic and structural basis of the interaction between proteins and carbohydrates from a fundamental point of view in several biologically relevant systems. Atomic-level demonstration, for the first time, of the full and reversible refolding of a transmembrane protein into a water-soluble form by employing sugar-containing detergents. Atomic-level demonstration, for the first time, of the binding of a carbohydrate to a pore-forming toxin (FraC) using its lipid binding module. Elucidation of the recognition mechanism of the glycoprotein Env of HIV-1 by a broadly-neutralizing anti-HIV-1 antibody at the atomic level. Demonstration that the terminal galactose of the glycan attached to the Fc region of IgG modulate the effector function of IgG. And explanation of the thermodynamic role of the glycan attached to residue Asn297 of the Fc region of IgG was revealed.
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