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Membrane docking mode of the C2 domain of PKCε: An infrared spectroscopy and FRET study

Journal article
Authors A. Ausili
Mattias Berglin
Hans-Björne Elwing
A. L. Egea-Jiménez
S. Corbalán-García
J. C. Gómez-Fernández
Published in Biochimica et Biophysica Acta - Biomembranes
Volume 1828
Issue 2
Pages 552-560
ISSN 0005-2736
Publication year 2013
Published at Department of Chemistry and Molecular Biology
Pages 552-560
Language en
Links dx.doi.org/10.1016/j.bbamem.2012.10...
Keywords ATR-IR, C2 domains, Membrane docking, PKCε, 1 palmitoyl 2 oleoyl sn glycero 3 phosphate, 1 palmitoyl 2 oleoyl sn glycero 3 phosphoethanolamine, 2 oleoyl 1 palmitoylphosphatidylcholine, cardiolipin, glycerophospholipid, protein kinase C epsilon, unclassified drug, article, artificial membrane, cell membrane, controlled study, enzyme binding, enzyme structure, fluorescence resonance energy transfer, infrared spectroscopy, lipid bilayer, lipid composition, mathematical computing, membrane structure, mitochondrial membrane, molecular docking, priority journal, protein binding, protein lipid interaction, protein secondary structure, Adenosine, Calcium, Glycerophospholipids, Humans, Lipid Bilayers, Lipids, Mitochondrial Membranes, Models, Molecular, Models, Statistical, Molecular Conformation, Phosphatidylcholines, Phosphatidylethanolamines, Phospholipids, Protein Conformation, Protein Kinase C-epsilon, Protein Structure, Secondary, Protein Structure, Tertiary, Spectrophotometry, Infrared
Subject categories Biochemistry

Abstract

The C2 domain of PKCε binds to negatively charged phospholipids but little is known so far about the docking orientation of this domain when it is bound. By using a FRET assay we have studied the binding of this domain to model membranes. We have also used ATR-Fourier transform infrared spectroscopy with polarized light (ATR-FTIR) to determine the docking mode by calculating the β-sandwich orientation when the domain is bound to different types of model membranes. The vesicle lipid compositions were: POPC/POPE/POPA (22:36:42) imitating the inner leaflet of a plasma membrane, POPC/POPA (50:50) in which POPE has been eliminated with respect to the former composition and POPC/POPE/CL (43:36:21) imitating the inner mitochondrial membrane. Results show that the β-sandwich of the PKCα-C2 domain is inclined at an angle α close to 45 to the membrane normal. Some differences were found with respect to the extent of binding as a function of phospholipid composition and small changes on secondary structure were only evident when the domain was bound to model membranes of POPC/POPA: in this case, the percentage of β-sheet of the C2 domain increases if compared with the secondary structure of the domain in the absence of vesicles. With respect to the β-sandwich orientation, when the domain is bound to POPC/POPE/CL membranes it forms an angle with the normal to the surface of the lipid bilayer (39) smaller than that one observed when the domain interacts with vesicles of POPC/POPA (49). © 2012 Elsevier B.V. All rights reserved.

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