| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2017: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2016: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Outline of Final Research Achievements |
To understand the function of negative-ring structures by D552 and D556 of the Aplysia FMRFamide-gated Na+ channel (AkFaNaC), the mutant channels (D552N, D556N, D552ND556N) were made and examined in Xenopus oocytes. We found that the Ca2+ coordination to D552 and D556 inhibits the activation of FaNaC. We constructed an allosteric model in which the channels are in either Ca2+-unbound or Ca2+-bound states. The model explains many aspects of the activation of AkFaNaC. To extend the research, we examined seven SS bonds in the external domain of FaNaC which must be important for maintaining the inner space of the external domain of FaNaC. We also started to analyze the functional impact of the negative-rings of the rat acid-sensing ion channel which are structurally similar to the negative-rings of FaNaC.
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