| Project/Area Number |
20790030
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Physical pharmacy
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| Research Institution | The University of Tokyo |
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Principal Investigator |
NISHIDA Noritaka The University of Tokyo, 大学院・薬学系研究科, 助教 (50456183)
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| Project Period (FY) |
2008 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2009: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2008: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 構造生物学 / NMR / 血小板凝集 / VWF / ADAMTS-13 |
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| Research Abstract |
Von Willebrand factor (VWF) mediates platelet adhesion under high shear stress. The activity of VWF is controlled by the ADAMTS13, which cuts the VWF in the force dependent manner. However, the structural basis as to how VWF exposes the cryptic site in the A2 domain for ADAMTS13 is unknown. In this study, I made a recombinant VWF A2 domain, using Pichia Pastorsis. Backbone resonance assignment of A2 domain was established for >80% signals. Based on the chemical shift change induced by low concentration of urea, the a3 and a5 helices and a4less loop, which is proximal to the scissile bond, undergoes a conformational change that would exposes the cleavage site for ADAMTS13.
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