| Project/Area Number |
60430031
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| Research Category |
Grant-in-Aid for General Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
結晶学
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| Research Institution | Nagoya University |
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Principal Investigator |
ASHIDA Tamaichi Nagoya University, Faculty of Engineering Professor, 工学部, 教授 (10029936)
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| Co-Investigator(Kenkyū-buntansha) |
TANAKA Isao Hokkaido University, Faculty of Science Associate Professor, 理学部, 助教授 (70093052)
YAMANE Takashi Nagoya University, Faculty of Engineering Associate Professor, 工学部, 助教授 (80030055)
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| Project Period (FY) |
1985 – 1986
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| Project Status |
Completed (Fiscal Year 1986)
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| Budget Amount *help |
¥18,500,000 (Direct Cost: ¥18,500,000)
Fiscal Year 1986: ¥2,500,000 (Direct Cost: ¥2,500,000)
Fiscal Year 1985: ¥16,000,000 (Direct Cost: ¥16,000,000)
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| Keywords | Crystal Structure of Bowman-Birk Inhibitor / Crystal Structure of the Trypsin- Bowman-Birk Inhibitor / Bowman-Birk Inhibitor / ボーマン・バーク型インヒビター / インヒビターの結晶構造 / 蛋白質分解酵素 / ボーマンバーク型インヒビター / トリプシン阻害蛋白質 / 蛋白質結晶構造解析 / 結晶構造解析 / トリプシン・インヒビター複合体 |
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| Research Abstract |
The structure analyses of a family of the Bowman-Birk type protease inhibitors and their complexes with proteases have successfully been carried out. The Bowman-Birk inhibitors which inhibit serine proteases are small proteins with 60-80 amino acid residues. An inhibitor molecule has seven disulfide bridges, and contains very few hydrophobic residues. It consists of two domains, of which the amino acid sequences are very similar to each other.
1. 2.3 A structure analysis of the trypsin-AB-I (azuki bean inhibitor) complex: Azuki bean inhibitor AB-I inhibits trypsin and chymotrypsin. The complex between AB-I and trypsin (1:1) gave fine crystals suitable for the X-ray analysis. Of the inhibitor only the trypsin-binding domain could be determined. Including 140 water molecules, R = 0.20. The binding site of the inhibitor including Lys26 is tightly bound in the trypsin active center by several hydrogen bonds and van der Waals contacts. The structure of the binding site of the inhibitor seems to be very stable, and any deviation from the stable structure which is necessary to induce a proteolytic reaction seems hardly to occur.
2. 3.3 A analysis of peanut inhibitor A-II: The inhibitor molecule has the dimension of 45x15x15 A, and consists of two distinct domains of which the structures are very similar with each other. Their structures are also essentially the same as that of the AB-I trypsin-binding domain. The two domains are related by an intramolecular pseudo twofold axis, and linked by two rather flexible peptide chains, and each domain has one binding site for proteases at the edges of the molecule.
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