Structural basis for the drug binding of human alpha1-acid glycoprotein
| Project/Area Number |
23790052
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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 | Kumamoto University |
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Principal Investigator |
NAKAMURA Teruya 熊本大学, 大学院・生命科学研究部, 助教 (40433015)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2012: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2011: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | 薬物結合蛋白質 / 構造活性相関 / X線結晶構造解析 / Ｘ線結晶構造解析 |
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| Research Abstract |
Human a1-acid glycoprotein binds to a variety of drugs and therebyregulates their tissue distribution. AGP exists as a mixture of two genetic variants,the A and F1*S variants, which bind drugs with different selectivities. In this study,we determined crystal structures of the A variant in complex with two types of tricyclicdrugs, and revealed their binding modes in the pocket of the A variant. Also, we mutatedthe amino acid residues which are involved in drug binding, and examined the bindingproperties of the mutants.
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Report
(3 results)
Research Products
(18 results)
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[Journal Article] Crystallization and preliminary X-ray analysis of human MTH1 with a homogeneous N-terminus.2013
Author(s)
Koga Y, Inazato M, Nakamura T, Hashikawa C, Chirifu M, Michi A, Yamashita T, Toma S, Kuniyasu A, Ikemizu S, Nakabeppu Y, Yamagata Y.
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Journal Title
Acta Crystallogr Sect F Struct Biol Cryst Commun
Volume: 69(Pt 1)
Issue: 1
Pages: 45-48
DOI
Related Report
Peer Reviewed
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