| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2013: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2012: ¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
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| Outline of Final Research Achievements |
Spatially separated sites in a protein molecule communicate by intramolecular allosteric interactions, which generally regulate protein activities. To investigate the detailed molecular mechanisms of intramolecular allosteric interactions, the phospholipase C-δ1 (PLC-δ1) pleckstrin homology (PH) domain and M-ficolin are employed as model proteins. By the NMR and Native-PAGE analyses of the PLC-δ1 PH domain, it was found that some side chains in the protein mediate the allosteric interactions, which regulate the ligand-binding activity. As the first step to investigate the intramolecular allosteric interactions in M-ficolin, we assigned the backbone NMR signals of the monomeric M-ficolin recognition domain, suggesting that the secondary structure predicted by the assignments is similar to that of the trimeric protein in the crystal.
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