Structural Analysis of Inhibitor Binding Site of Enzyme by Neutron Crystallography
Project/Area Number |
23770129
|
Research Category |
Grant-in-Aid for Young Scientists (B)
|
Allocation Type | Multi-year Fund |
Research Field |
Structural biochemistry
|
Research Institution | Japan Atomic Energy Agency |
Principal Investigator |
ADACHI Motoyasu 独立行政法人日本原子力研究開発機構, 原子力科学研究部門・量子ビーム応用研究センター, 研究副主幹 (60293958)
|
Project Period (FY) |
2011 – 2013
|
Project Status |
Completed (Fiscal Year 2013)
|
Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2013: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2012: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2011: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
Keywords | HIV / プロテアーゼ / 結晶構造解析 / 中性子 / 結晶 / 構造解析 |
Research Abstract |
Human immune deficiency virus protease–I (HIVPR) is one of the important drug target proteins for the acquired immune deficiency syndrome. For the efficient drug discovery, it is of importance to obtain structural information of bound water molecules at the active site of HIVPR for the binding of potent inhibitors. Since HIVPR involves the self-degradation, the single-chained and cross-linked HIVPR were designed. The both HIVPR were prepared, and their tertiary structure was determined by X-ray crystallography. The designed HIV-PR will be useful for evaluate the affinity of newly designed inhibitors from kinetic and thermodynamic point of view and preparation of large crystal for neutron crystallography.
|
Report
(4 results)
Research Products
(11 results)