2014 Fiscal Year Final Research Report
Molecular basis of P-type ion pumps and diseases caused by pump defects.
| Project/Area Number |
23370058
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Asahikawa Medical College |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
YAMASAKI Kazuo 旭川医科大学, 医学部, 講師 (60241428)
DAIHO Takashi 旭川医科大学, 医学部, 准教授 (90207267)
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| Project Period (FY) |
2011-04-01 – 2015-03-31
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| Keywords | P型カチオン輸送ATPase / Ca-ATPase / リン酸化反応中間体 / 反応中間体構造アナログ / 筋小胞体 / 能動輸送 / エネルギー共役 / 反応機構 |
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| Outline of Final Research Achievements |
P-type ATPases possess common domain-structure and couple the ATP hydrolysis with the specific cation-transport. In this study, we first revealed by extensive mutations and kinetic analyses of Ca-ATPase that the second transmembrane helix plays critical roles via its motions and changes in its secondary structure for transferring the motions of cytoplasmic domains to the transmembrane cation transport sites there by for the energy coupling. We also revealed that unique structural fluctuation is equipped in each of the phosphoenzyme intermediates, and the fluctuation functions to accomplish the proper forward transport reaction. Thus we contributed to the comprehensive understanding of the P-type ATPase mechanism and an establishment of molecular basis for diseases developed by the pump defects.
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| Free Research Field |
生化学
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