Structure-activity relationship of carcinogenic factor, Tip-alpha, from Helicobacter pylori
Project/Area Number |
26840052
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Biophysics
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Research Institution | Kyoto Sangyo University |
Principal Investigator |
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Co-Investigator(Renkei-kenkyūsha) |
TSUGE Hideaki 京都産業大学, 総合生命科学部, 教授 (40299342)
IKEGUCHI Masamichi 創価大学, 理工学部, 教授 (00192477)
|
Project Period (FY) |
2014-04-01 – 2016-03-31
|
Project Status |
Completed (Fiscal Year 2015)
|
Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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Keywords | ピロリ菌 / 胃がん / X線結晶構造解析 / X線小角散乱 |
Outline of Final Research Achievements |
TNFα inducing protein (Tipα) is secreted by Helicobacter pylori and it induces gastritis and gastric cancer. Tipα forms homo-dimer with two disulfide bonds via two cysteine residues at N-terminus. I and colleagues revealed the crystal structure of N-terminus deletion mutant (del-Tipα). Based on our del-Tipα structure and other Tipα and del-Tipα structures, Tipα forms the open dimer to closed one at acidic and neutral condition, respectively. In this study, we evaluated the dimer formations of Tipα and del-Tipα by small angle X-ray scattering technique. The results indicated that the dimer formations in the crystals at both acidic and neutral pH are same as the formations in the solution, and furthermore, the dimer of Tipα at neutral condition, which has not been revealed, is the closed-form dimer.
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Report
(3 results)
Research Products
(1 results)