| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2014: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Outline of Final Research Achievements |
Neutron crystal structure of human farnesyl pyrophosphate synthase (FPPS) in complex with risedronate (RIS) was determined, and the protonation state and hydration of RIS were elucidated. The structural analysis revealed that the phosphate groups of RIS were fully deprotonated with the abnormally decreased pKa. In addition, it was suggested that the roles of E93 and D264 consisted of canceling the extra negative charges upon the binding of ligands. This information would be helpful for the development of non-bisphosphonate FPPS inhibitors.
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