| Project/Area Number |
05403031
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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 |
Applied molecular and cellular biology
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| Research Institution | The University of Tokyo |
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Principal Investigator |
SUZUKI Akinori The University of Tokyo, Faculty Agriculture, Professor, 農学部, 教授 (90011907)
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| Co-Investigator(Kenkyū-buntansha) |
KATAOKA Hiroshi The University of Tokyo, Faculty of Agriculture, Associate Professor, 農学部, 助教授 (60202008)
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| Project Period (FY) |
1993 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥38,800,000 (Direct Cost: ¥38,800,000)
Fiscal Year 1995: ¥7,000,000 (Direct Cost: ¥7,000,000)
Fiscal Year 1994: ¥14,700,000 (Direct Cost: ¥14,700,000)
Fiscal Year 1993: ¥17,100,000 (Direct Cost: ¥17,100,000)
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| Keywords | NMR / Tertiary structure / PTTH / Insulin / インスリン族ペプチド / ボンビキシン / 昆虫神経ペプチド / 前胸腺刺激ホルモン / 昆虫 / ペプチド |
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| Research Abstract |
1.The tertiary structure of bombyxin was determined by the NMR method.
2.From the bioassay of chimeric molecules of bombyxin and insulin, the central part of B-chain, TyrB6-LeuB18, is found to be very important for bombyxin activity.
3.Solution structure determination of these chimeric molecules revealed that their B-chain central parts took similar main-chain conformation, but formed dissimilar patches on their molecular surface. Therefore, the surface patch formed by the central part of the bombyxin B-chain is of critical importance for recognition of bombyxin receptor.
4.NMR data of PTTH revealed that the central part of PTTH has rigid structure and is rich in beta-sheet.
5.Molecular modeling of PTTH by computer suggested that PTTH has two b-sheets and is belong to the cystine knot superfamily.
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