2017 Fiscal Year Final Research Report
Structural analysis of the deregulation mechanism of SHP2 phosphatase by Helicobacter pylori CagA
Project/Area Number |
16K19130
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Bacteriology (including mycology)
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Research Institution | High Energy Accelerator Research Organization |
Principal Investigator |
Nagase Lisa 大学共同利用機関法人高エネルギー加速器研究機構, 物質構造科学研究所, 研究員 (60768034)
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Project Period (FY) |
2016-04-01 – 2018-03-31
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Keywords | CagA / ピロリ菌 |
Outline of Final Research Achievements |
In this study, a crystal of complex of EPIYA-D peptide derived from Helicobacter pylori CagA protein and N-SH2 domain of SHP2 was obtained and X-ray diffraction experiment was performed. As a result of analyzing the data, it was confirmed that this crystal was a complex of EPIYA-D peptide and N-SH2. Through this study, it was found that the crystal of the complex of peptide and SH2 was obtained, which is extremely useful for research to elucidate the molecular basis of SHP2 activation by CagA.
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Free Research Field |
生化学、構造生物学
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