Structure and dynamics of the phospholipase C-delta1 pleckstrin homology domain located at the lipid bilayer surface |
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Authors: | Tuzi Satoru Uekama Naoko Okada Masashi Yamaguchi Satoru Saito Hazime Yagisawa Hitoshi |
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Affiliation: | Department of Life Science, Himeji Institute of Technology, Harima Science Garden City, Kouto 3-chome, Kamigori, Hyogo 678-1297, Japan. tuzi@sci.himeji-tech.ac.jp |
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Abstract: | Despite the importance of signal transduction pathways at membrane surfaces, there have been few means of investigating their molecular mechanisms based on the structural information of membrane-bound proteins. We applied solid state NMR as a novel method to obtain structural information about the phospholipase C-delta1 (PLC-delta1) pleckstrin homology (PH) domain at the lipid bilayer surface. NMR spectra of the alanine residues in the vicinity of the beta5/beta6 loop in the PH domain revealed changes in local conformations due to the membrane localization of the protein. We propose that these conformational changes originate from a hydrophobic interaction between the amphipathic alpha-helix located in the beta5/beta6 loop and the hydrophobic layer of the membrane and contribute to the membrane binding affinity, interdomain interactions and intermolecular interactions of PLC-delta1. |
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