| Project/Area Number |
06305006
|
|---|
| Research Category |
Grant-in-Aid for Co-operative Research (A)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
広領域
|
|---|
| Research Institution | University of Tokyo |
|---|
Principal Investigator |
SATOW Yoshinori University of Tokyo, Faculty of Pharmaceutical Sciences, Professor, 薬学部, 教授 (30150014)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
FUKUYAMA Keiichi Osaka University, Faculty of Science, Professor, 理学部, 教授 (80032283)
TSUKIHARA Tomitake Osaka University, Institute for Protein Research, Professor, 蛋白質研究所, 教授 (00032277)
MIKI Kunio University of Kyoto, Graduate School of Science, Professor, 大学院理学研究科, 教授 (10116105)
TANAKA Isao Hokkaido University, Graduate School of Science, Professor, 理学部, 教授 (70093052)
TANAKA Nobuo Tokyo Institute of Technology, Faculty of Bioscience and Biotechnology, Professo, 生命理工学部, 教授 (50032024)
山根 隆 名古屋大学, 工学部, 助教授 (80030055)
藤井 敏 大阪大学, 薬学部, 助教授 (10107104)
|
|---|
| Project Period (FY) |
1994 – 1995
|
| Project Status |
Completed (Fiscal Year 1995)
|
| Budget Amount *help |
¥9,300,000 (Direct Cost: ¥9,300,000)
Fiscal Year 1995: ¥4,400,000 (Direct Cost: ¥4,400,000)
Fiscal Year 1994: ¥4,900,000 (Direct Cost: ¥4,900,000)
|
|---|
| Keywords | Proteins / X-ray crystallography / Structural biology / Membrane protein / Glycoprotein / Antibody / Crystal structure / Antigen recognition / X線結晶構造解析 / 膜蛋白質 / 蛋白質三次元構造 / 結晶構造 / 生体高分子 / X線回折法 / 分子生物学 |
|---|
| Research Abstract |
This research project aimed at the development of rapid and accurate methods for macromolecular X-ray crystallography, through collaborative studies of three-dimensional structures and functions of proteins. The project was carried out by 15 investigators.
The proteins studied in the project were, genetically engineered proteins with amino-acid substitutions, proteolytic and glycolytic enzymes as well as their complexes with inhibitors, proteins that recognize nucleic acids, antibodies and their complexes with haptens, membrane proteins, viruses, and glycoproteins. The methods and techniques developed were, for engineering and preparation of protein specimens, for crystallization of proteins, for determination of very large structural units, for diffraction data collection, for utilization of anomalous scattering effects, for automated molecular-replacement solutions, and for utilization of other structural information.
Structure determinations of a membrane protein of bovine cytochrome c oxidase and a glycoprotein of human renal dipeptidase are typical examples of the successful results. The former protein was crystallized and solved with the techniques developed. The later were prepared with genetic engineering and enzymatic deglycosylation techniques. The structures of chimeric enzymes, proteinases of a trypsin family, and unliganded and hapten-liganded forms of Fab and Fv fragments of antibodies were also determined. The developments of hardware and software systems with rapid and accurate data collection capabilities, of techniques for locating anomalous scatterers and for MAD analyzes, and of automated molecular-replacement procedures were carried out.
In each year, a meeting for exchanging information about research activities of investigators was held. A report on research activities, progresses, and achievements was published at the end of each year. The report for the final year was circulated to researchers in related fields.
|
