Elucidation of activation mechanism of human acetyl-CoA carboxylase
| Project/Area Number |
22590113
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Drug development chemistry
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
KUNISHIMA Naoki 独立行政法人理化学研究所, タンパク質結晶構造解析研究グループ, グループ副ディレクター (70415149)
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| Co-Investigator(Renkei-kenkyūsha) |
MATSUURA Yoshinori 独立行政法人理化学研究所, タンパク質結晶構造解析研究グループ, リサーチアソシエイト (50513462)
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| Project Period (FY) |
2010 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
Fiscal Year 2012: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2011: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2010: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
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| Keywords | 生活習慣病 / 脂肪酸生合成 / 結晶構造解析 / X線回折 / 酵素 / タンパク質 / 立体構造 / 薬物設計 |
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| Research Abstract |
Toward the elucidation of the activation mechanism of acetyl-CoA carboxylase (ACC) that catalyzes the rate-limiting step of the fatty-acid biosynthesis, we tried the protein crystallography of the central domain of human ACC (hBCCP1, hBCCP2) and its activation enzyme biotin protein ligase (hBPL). The genes were synthesized for a large-scale expression using E.coli. These proteins were generally expressed as inclusion bodies that could not be solubilized by methods including the denaturation/refolding and the substitution of cysteine with alanine.
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Report
(4 results)
Research Products
(4 results)
