| Project/Area Number |
11480189
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Biophysics
|
|---|
| Research Institution | Nagoya University |
|---|
Principal Investigator |
GO Mitiko Nagoya University, Department of Biology, Faculty of Science, Professor, 大学院・理学研究科, 教授 (70037290)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
YURA Kei Japan Atomic Energy Research Institute, Center for promotion of Computational Science and Engineering, Researcher, 計算科学技術推進センター, 研究員 (50252226)
TAKAHASHI Ken-ichi Nagoya University, Department of Biology, Faculty of Science, Assistant, 大学院・理学研究科, 助手 (20322737)
|
|---|
| Project Period (FY) |
1999 – 2002
|
| Project Status |
Completed (Fiscal Year 2002)
|
| Budget Amount *help |
¥14,500,000 (Direct Cost: ¥14,500,000)
Fiscal Year 2002: ¥2,500,000 (Direct Cost: ¥2,500,000)
Fiscal Year 2001: ¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2000: ¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 1999: ¥5,000,000 (Direct Cost: ¥5,000,000)
|
|---|
| Keywords | Module classification / shuffling / Intron / Membrane protein / peroxiclase / Metal ion / Nucleic acid interaction / Function finetuning / ペルオキシダーゼ / モジュール / ゲノム情報 / ヘモグロビン / サブユニット接触 / タンパク質機能 / モジュールシャッフリング / タンパク質相互作用 / 金属イオン結合 / ミニバルナ-ゼ / フィコシアニン / リン酸基結合 / キシラナーゼ / キメラ酵素 / 糖結合 / 3Dキーノート |
|---|
| Research Abstract |
The aim of this study is (1) to clarify that key components of protein functions are localized to compact short segments, modules, and (2) to elucidate principle of protein design using modules as building blocks. In consequence, we found various kinds of protein functions were assigned to modules. For example, (1) the functional sites of the catalytic domain of family 10 xylanase are localized to some of the modules; (2) in many case, ligands for certain metal ions exist within one or two modules. Furthermore, modules with similar structure and function are frequently observed in various proteins, which indicates the possibility that the modules were shuffled. In addition, (3) common modules are found to be used for protein-protein interaction; (4) only two modules are used in subunit interaction of hemoglobin, which could explain why subunit interactions of hemoglobin are diversified in various lineage. We also showed that modules can be deleted or shuffled by experiments. For example, (1) module M2 in barnase was deleted without loss of the stable three-dimensional structure similar to the native structure and the cooperative folding behavior. (2) a chimera xylanase, which was made by exchange of module M10 between two kinds of xylanases in family 10, maintained the structure and function, though the enzyme activity decrease by a tenth. This study has clarified a basic principle for module-based protein design from both views of computer science and experimental science.
|
