TAILIEUCHUNG - Báo cáo khoa học: Phosphatidylserine induces functional and structural alterations of the membrane-associated pleckstrin homology domain of phospholipase C-d1

The membrane binding affinity of the pleckstrin homology (PH) domain of phospholipase C (PLC)-d1 was investigated using a vesicle coprecipitation assay and the structure of the membrane-associated PH domain was probed using solid-state 13 C NMR spectroscopy. | ỊFEBS Journal Phosphatidylserine induces functional and structural alterations of the membrane-associated pleckstrin homology domain of phospholipase C-Ô1 Naoko Uekama Takio Sugita Masashi Okada Hitoshi Yagisawa and Satoru Tuzi Graduate Schoolof Life Science University of Hyogo Harima Science Garden City Kamigori Hyogo Japan Keywords cellular signal transduction phosphatidylserine phospholipase C-81 pleckstrin homology domain Correspondence S. Tuzi Graduate School of Life Science University of Hyogo Harima Science Garden City Kouto 3-chome Kamigori Hyogo 6781297 Japan Fax 81 791 580182 Tel 81 791 580180 E-mail tuzi@ Received 4 August 2006 revised 1 November 2006 accepted 6 November 2006 doi The membrane binding affinity of the pleckstrin homology PH domain of phospholipase C PLC -Ỗ1 was investigated using a vesicle coprecipitation assay and the structure of the membrane-associated PH domain was probed using solid-state 13C NMR spectroscopy. Twenty per cent phosphatidylserine PS in the membrane caused a moderate but significant reduction of the membrane binding affinity of the PH domain despite the predicted electrostatic attraction between the PH domain and the head groups of PS. Solid-state NMR spectra of the PH domain bound to the phosphatidylcholine PC PS phosphatidylinositol 4 5-bisphosphate PIP2 75 20 5 vesicle indicated loss of the interaction between the amphipathic a2-helix of the PH domain and the interface region of the membrane which was previously reported for the PH domain bound to PC PIP2 95 5 vesicles. Characteristic local conformations in the vicinity of Ala88 and Ala112 induced by the hydrophobic interaction between the a2-helix and the membrane interface were lost in the structure of the PH domain at the surface of the PC PS PIP2 vesicle and consequently the structure becomes identical to the solution structure of the PH domain bound to D-myo-inositol 1 4 5-trisphosphate. These local structural .

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