| 研究課題/領域番号 |
15K06962
|
|---|
| 研究機関 | 東京大学 |
|---|
研究代表者 |
CAAVEIRO Jose 東京大学, 工学(系)研究科(研究院), 研究員 (00536732)
|
|---|
| 研究期間 (年度) |
2015-04-01 – 2018-03-31
|
| キーワード | Glycan / Sugar / Antibody / Enzyme / Pore forming protein / X-ray Crystallography / Thermodynamics / Kinetics |
|---|
| 研究実績の概要 |
1. Data collection and analysis of proteins GalM, FraC, and other systems in which sugars play an important role such as antibodies. These data were necessary to make progress in the project according to the plan described last year. Specifically the crystallographic, enzymatic, mutagenesis and biophysical analysis work have progressed adequately and we are ready to start the preparation of more manuscripts describing these results.
2. Presentation of data at two international conferences (Pacifichem2015) and a Gordon Conference. These two meetings were ideal to publicize our research and to get feedback from senior researchers in the field. I made contacts with some of these researchers with the goal of establishing international collaborations.
3. Publication of three manuscripts in highly regarded international journals, highlighting our work and facilitating the graduation of a Ph.D. student (also winner of the 6th Ikushi Prize 【育志賞】).
|
| 現在までの達成度 (区分) |
現在までの達成度 (区分)
2: おおむね順調に進展している
理由
1. Data acquisition and analysis is progressing well, specially for the pore forming protein FraC. The goals for the fiscal year 2015 were achieved.
2. Data was published in scientific journals as described elsewhere, and presented at international conferences.
|
| 今後の研究の推進方策 |
1. GalM. In particular I will analyze more structural, thermodynamic and functional data. The use of sugar containing an atom of sulfur (thio-sugars) will enlighten the selectivity and prowess of the enzyme. These results will be summarized in two manuscripts to be submitted to international per-reviewed journals and presented at an international conference.
2. Characterize the sugar binding and function of FraC. We have already identified some sugars binding to a shared binding site, and our goal is to determine the exact position of that binding site in the architecture of the protein, and the importance for its function. I would like to employ bioinformatic techniques to understand the generality of these findings. These results will also be summarized in one or two manuscripts to be submitted to international per-reviewed journals and presented at international conferences.
|
