| Project/Area Number |
24790057
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Physical pharmacy
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| Research Institution | Hyogo University of Health Sciences |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
|
| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Keywords | X線結晶解析 / X線溶液散乱 / 宇宙実験 / タンパク質 / コラーゲン / 基質認識 / 地球環境 / CD |
|---|
| Research Abstract |
Proline-specific aminopeptidases are critical to the degradation of proline-rich peptides and proteins, such as collagen and its denatured form, gelatin. Collagens are the largest components in animal tissues and the most major hard-to-degrade proteins because of their unique fibrils composed of triple helical wound polypeptides. In this study, we crystallized three of the recombinant enzymes (Pz-A, Pz-B, and AM-1), and performed its preliminary X-ray crystallographic analysis. We have determined the entire structure of the these aminopeptidases, found a very unique apical domain sharing the interface with a domain containing a main active site and described about the characteristic structure and mechanism for the substrate recognition for proly peptides.
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