ANALYSIS TRP TYPE Ca^<2+> CHANNEL COVALENTLY ATTACHED WITH KINASE DOMAIN
| Project/Area Number |
12670039
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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 |
General physiology
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| Research Institution | OKAYAMA UNIVERSITY |
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Principal Investigator |
MATSUSHITA Masyuki Graduate School of Medicine and Dentistry, Okayama University, Assistant, 大学院・医歯学総合研究科, 助手 (30273965)
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| Co-Investigator(Kenkyū-buntansha) |
MATSUI Hideki Graduate School of Medicine and Dentistry, Okayama University, Professor, 大学院・医歯学総合研究科, 教授 (30157234)
MORIWAKI Akiyoshi Graduate School of Medicine and Dentistry, Okayama University, Assistant Professor, 大学院・医歯学総合研究科, 助教授 (10144742)
TOMIZAWA Kazuhito Graduate School of Medicine and Dentistry, Okayama University, Lecturer, 大学院・医歯学総合研究科, 講師 (40274287)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2001: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2000: ¥2,100,000 (Direct Cost: ¥2,100,000)
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| Keywords | ChaK / Trp channel / tongue / Calcium / Kinase / Zinc finger / Crystal Structurre / ATP / Chak / Zinc finger |
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| Research Abstract |
A search of EST data bases indicated that there were a number of identified cDNA sequences that were related to the catalytic domain of EF2K. These included genes for EF2K and myosin heavy chain kinase (MHCK) from several species. One novel gene was identified that was distinct from EF2K and MHCK, and this was cloned by library screening from mouse embryo. The full length of this clone was sequenced and found 200kDa protein, designated Channel Kinase (ChaK), which has homology to the TRP channel and kinase domain of EF2K family. The Catalytic domain of Chak was expressed in E.coli and found also to be a Ser/Thr protein kinase. The results obtained suggest that EF2K and ChaK are members of a family of protein kinases that is distinct from the classical protein kinases. The structure of the kinase domain reveals unexpected similality to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP grasp domains.
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Report
(3 results)
Research Products
(18 results)
