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Membrane docking mo...
Membrane docking mode of the C2 domain of PKCε: An infrared spectroscopy and FRET study
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Ausili, A. (author)
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- Berglin, Mattias, 1970 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology
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- Elwing, Hans-Björne, 1946 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology
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Egea-Jiménez, A. L. (author)
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Corbalán-García, S. (author)
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Gómez-Fernández, J. C. (author)
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(creator_code:org_t)
- Elsevier BV, 2013
- 2013
- English.
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In: Biochimica et Biophysica Acta - Biomembranes. - : Elsevier BV. - 0005-2736. ; 1828:2, s. 552-560
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Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- 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
Publication and Content Type
- ref (subject category)
- art (subject category)
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