Intramolecular allosteric interactions in proteins
Project/Area Number |
24570190
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Biophysics
|
Research Institution | National Institute of Infectious Diseases (2014) Institute for Molecular Science (2012-2013) |
Principal Investigator |
TANIO Michikazu 国立感染症研究所, 血液・安全性研究部, 主任研究官 (10416662)
|
Project Period (FY) |
2012-04-01 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2013: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2012: ¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
|
Keywords | 分子内情報伝達 / タンパク質 / 相互作用 / NMR / 分子内アロステリー / PHドメイン / フィコリン / native PAGE / 分子内アロステリック効果 / 熱安定性 |
Outline of Final Research Achievements |
Spatially separated sites in a protein molecule communicate by intramolecular allosteric interactions, which generally regulate protein activities. To investigate the detailed molecular mechanisms of intramolecular allosteric interactions, the phospholipase C-δ1 (PLC-δ1) pleckstrin homology (PH) domain and M-ficolin are employed as model proteins. By the NMR and Native-PAGE analyses of the PLC-δ1 PH domain, it was found that some side chains in the protein mediate the allosteric interactions, which regulate the ligand-binding activity. As the first step to investigate the intramolecular allosteric interactions in M-ficolin, we assigned the backbone NMR signals of the monomeric M-ficolin recognition domain, suggesting that the secondary structure predicted by the assignments is similar to that of the trimeric protein in the crystal.
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Report
(4 results)
Research Products
(13 results)