About: The Structure of Myristoylated Mason-Pfizer Monkey Virus Matrix Protein and the Role of Phosphatidylinositol-(4,5)-Bisphosphate in Its Membrane Binding     Goto   Sponge   NotDistinct   Permalink

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  • We determined the solution structure of myristoylated Mason-Pfizer monkey virus matrix protein by NMR spectroscopy. The myristoyl group is buried inside the protein and causes a slight reorientation of the helices. This reorientation leads to the creation of a binding site for phosphatidylinositols. The interaction between the matrix protein and phosphatidylinositols carrying C-8 fatty acid chains was monitored by observation of concentration-dependent chemical shift changes of the affected amino acid residues, a saturation transfer difference experiment and changes in P-31 chemical shifts. No differences in the binding mode or affinity were observed with differently phosphorylated phosphatidylinositols. The structure of the matrix protein phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P-2] complex was then calculated with HADDOCK software based on the intermolecular nuclear Overhauser enhancement contacts between the ligand and the matrix protein obtained from a C-13-filtered/C-13-edited nuclear Overhauser enhancement spectroscopy experiment. PI(4,5)P-2 binding was not strong enough for triggering of the myristoyl-switch. The structural changes of the myristoylated matrix protein were also found to result in a drop in the oligomerization capacity of the protein.
  • We determined the solution structure of myristoylated Mason-Pfizer monkey virus matrix protein by NMR spectroscopy. The myristoyl group is buried inside the protein and causes a slight reorientation of the helices. This reorientation leads to the creation of a binding site for phosphatidylinositols. The interaction between the matrix protein and phosphatidylinositols carrying C-8 fatty acid chains was monitored by observation of concentration-dependent chemical shift changes of the affected amino acid residues, a saturation transfer difference experiment and changes in P-31 chemical shifts. No differences in the binding mode or affinity were observed with differently phosphorylated phosphatidylinositols. The structure of the matrix protein phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P-2] complex was then calculated with HADDOCK software based on the intermolecular nuclear Overhauser enhancement contacts between the ligand and the matrix protein obtained from a C-13-filtered/C-13-edited nuclear Overhauser enhancement spectroscopy experiment. PI(4,5)P-2 binding was not strong enough for triggering of the myristoyl-switch. The structural changes of the myristoylated matrix protein were also found to result in a drop in the oligomerization capacity of the protein. (en)
Title
  • The Structure of Myristoylated Mason-Pfizer Monkey Virus Matrix Protein and the Role of Phosphatidylinositol-(4,5)-Bisphosphate in Its Membrane Binding
  • The Structure of Myristoylated Mason-Pfizer Monkey Virus Matrix Protein and the Role of Phosphatidylinositol-(4,5)-Bisphosphate in Its Membrane Binding (en)
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  • The Structure of Myristoylated Mason-Pfizer Monkey Virus Matrix Protein and the Role of Phosphatidylinositol-(4,5)-Bisphosphate in Its Membrane Binding
  • The Structure of Myristoylated Mason-Pfizer Monkey Virus Matrix Protein and the Role of Phosphatidylinositol-(4,5)-Bisphosphate in Its Membrane Binding (en)
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  • RIV/60461373:22330/12:43894100!RIV13-GA0-22330___
http://linked.open...avai/riv/aktivita
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  • I, P(GAP302/12/1895), P(LH12011)
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  • 3
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  • 171894
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  • RIV/60461373:22330/12:43894100
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  • phosphatidylinositol; protein structure; myristoylated; M-PMV; retrovirus (en)
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  • GB - Spojené království Velké Británie a Severního Irska
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  • [41922A8F7118]
http://linked.open...i/riv/nazevZdroje
  • Journal of molecular biology
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  • 423
http://linked.open...iv/tvurceVysledku
  • Hrabal, Richard
  • Prchal, Jan
  • Ruml, Tomáš
  • Srb, Pavel
  • Hunter, Eric
http://linked.open...ain/vavai/riv/wos
  • 000310415400012
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  • 0022-2836
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  • 22330
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