Analysis of water and molecules bound to a prototypical GPCR
| Project/Area Number |
19370071
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Biophysics
|
|---|
| Research Institution | Gakushuin University |
|---|
Principal Investigator |
TETSUJI Okada Gakushuin University, 理学部, 教授 (10271545)
|
|---|
| Research Collaborator |
ODA Shunichiro 学習院大学, 理学部, 科研費技術員
RILEY Charles K. 学習院大学, 理学部, 科研費技術員
|
|---|
| Project Period (FY) |
2007 – 2009
|
| Project Status |
Completed (Fiscal Year 2009)
|
| Budget Amount *help |
¥13,520,000 (Direct Cost: ¥10,400,000、Indirect Cost: ¥3,120,000)
Fiscal Year 2009: ¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2008: ¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2007: ¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
|
|---|
| Keywords | 生物物理 / シグナル伝達 / 膜タンパク質 / 結晶構造 / 活性制御 / 膜蛋白質 |
|---|
| Research Abstract |
Activity of a G protein-coupled receptor (GPCR) is evoked upon agonist binding via yet unknown dynamics of the protein moiety. We have crystallized prototypical GPCR rhodopsin, in the presence of some retinal derivatives that would bind to the surface of the protein and affect the activity. The binding of β-ionone, which is a truncated form of retinal and is supposed to have some allosteric effect, has been detected by X-ray diffraction analysis to 2.6 angstroms resolution. This is the first example demonstrating that the hydrophobic surface of a GPCR could be occupied by a specifically bound small molecule.
|
Report
(4 results)
Research Products
(18 results)
