Intramolecular allosteric interactions in proteins

2014 Fiscal Year Final Research Report

• Project/Area Number: 24570190
• Research Category: Grant-in-Aid for Scientific Research (C)
• 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
• 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

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.

Free Research Field

生物物理