Molecular mechanism for divergent interactions in PAS domain proteins
| Project/Area Number |
23570194
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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 |
Biophysics
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| Research Institution | Nara Institute of Science and Technology |
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Principal Investigator |
YAMAZAKI Yoichi 奈良先端科学技術大学院大学, 物質創成科学研究科, 助教 (40332770)
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| Co-Investigator(Renkei-kenkyūsha) |
KAMIKUBO Hironari 奈良先端科学技術大学院大学, 物質創成科 学研究科, 准教授 (20311128)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2011: ¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
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| Keywords | 光生物学 / 情報伝達 / タンパク質間相互作用 / 光受容 |
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| Research Abstract |
There are many different functions even in a structurally homologous proteins. It is not clear how they realize these divergent functions on their same protein backbone. To evaluate these molecular divergent mechanism, two different PYP proteins classified as PAS domain proteins have been investigated about their molecular mechanism for structural changes and protein-protein interaction. As the results, (1) solution structure of the interaction protein for PYP has been identified. And then complex formation of this protein and PYP has been successfully identified. This complex was characteristic ring shape composed by hetero octamer. (2) a surface residue on the PYP has been identified as an interaction site. (3) X-ray crystal analysis for this PYP suggested that structural change was introduced around the interaction residue.
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Report
(4 results)
Research Products
(27 results)
