| Project/Area Number |
26440034
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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 | Tokyo University of Science (2016)
University of Shizuoka (2014-2015) |
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Principal Investigator |
YOKOYAMA HIDESHI 東京理科大学, 薬学部生命創薬科学科, 准教授 (70433208)
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| Co-Investigator(Kenkyū-buntansha) |
橋本 博 静岡県立大学, 薬学部, 教授 (40336590)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2016: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2015: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2014: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Keywords | 膜結合プロテアーゼ / ストマチン / OBドメイン / Ｘ線結晶構造 / Ｘ線結晶構造解析 / X線結晶構造 |
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| Outline of Final Research Achievements |
In humans, an absence of stomatin is associated with a form of hemolytic anemia known as hereditary stomatocytosis. In this study, I tried to elucidate how the partner protein STOPP (STomatin Operon Partner Protein) regulates the oligomeric protein stomatin. By X-ray crystallography, I elucidated that the protease domain of STOPP could form a different dimeric structure, and that the OB (Oligonucleotide Binding) domain of STOPP could assemble into 12-24 mer multimers based on a dimer as a basic unit. This result indicates that the OB domain functions as a scaffold protein to form the multimeric assembly of STOPP and stomatin. In the future, I want to elucidate the mechanism how hereditary stomatocytosis is developed.
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