| Project/Area Number |
18570184
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | University of Hyogo |
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Principal Investigator |
SATOU Tuzi University of Hyogo, Departrnent of Life Science, Associate Professor (60227387)
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| Co-Investigator(Kenkyū-buntansha) |
YAGISAWA Hitoshi University of Hyogo, Department of Life Science, Associate Professor (40192380)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥4,110,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥510,000)
Fiscal Year 2007: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2006: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | cellular signal transduction / lipid / molecular recognitior / PIP3 / spectroscopy / シグナル伝逹 |
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| Research Abstract |
In order to investigate molecular mechanisms of the cellular signal transduction pathways mediated by the PIP3-binding proteins at the membrane surfaces, spectroscopic techniques to examine molecular structures of the membrane binding allele at the membrane surfaces were developed. A sold state NMR spectroscopy and a UV resonance Raman spectroscopy were found to be suitable for this purpose, and were applied to of serve the structure of the PLC-δ1 PH domain, well-studied PIP_2-specific lipid binding domain, at the surface of lipid bilayer. The sold state ^<13>C NMR spectra showed that the conformation of the PH domain was altered at the membrane surface due to an interaction between the membrane interface and an amphipathic α-helix, and this conformational alteration is affected by the composition and curvature of the lipid bilayer. The UV resonance Raman spectra of the PH domain also provided structural information of sidechains of aromatic residues at the membrane surface, consistent with the data provided by the sold state ^<13>C WAR spectroscopy. On the basis of these findings, a PIP3-binding domain (SWAP-70 PH domain) was investigated. The UV resonance Raman spectroscopy provided spectra of SWAP-70 PH domain which can be interpreted by comparing with the data for the PLC-δ1 PH domain.
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