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Membrane docking mo...
Membrane docking mode of the C2 domain of PKCε: An infrared spectroscopy and FRET study
- Artikel/kapitelEngelska2013
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Nummerbeteckningar
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LIBRIS-ID:oai:gup.ub.gu.se/195351
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https://gup.ub.gu.se/publication/195351URI
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https://doi.org/10.1016/j.bbamem.2012.10.015DOI
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Ämneskategori:ref swepub-contenttype
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Ämneskategori:art swepub-publicationtype
Anmärkningar
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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.
Ämnesord och genrebeteckningar
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NATURVETENSKAP Biologi Biokemi och molekylärbiologi hsv//swe
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NATURAL SCIENCES Biological Sciences Biochemistry and Molecular Biology hsv//eng
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ATR-IR
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C2 domains
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Membrane docking
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PKCε
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1 palmitoyl 2 oleoyl sn glycero 3 phosphate
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1 palmitoyl 2 oleoyl sn glycero 3 phosphoethanolamine
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2 oleoyl 1 palmitoylphosphatidylcholine
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cardiolipin
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glycerophospholipid
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protein kinase C epsilon
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unclassified drug
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article
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artificial membrane
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cell membrane
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controlled study
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enzyme binding
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enzyme structure
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fluorescence resonance energy transfer
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infrared spectroscopy
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lipid bilayer
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lipid composition
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mathematical computing
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membrane structure
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mitochondrial membrane
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molecular docking
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priority journal
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protein binding
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protein lipid interaction
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protein secondary structure
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Adenosine
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Calcium
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Glycerophospholipids
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Humans
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Lipid Bilayers
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Lipids
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Mitochondrial Membranes
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Models
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Molecular
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Models
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Statistical
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Molecular Conformation
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Phosphatidylcholines
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Phosphatidylethanolamines
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Phospholipids
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Protein Conformation
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Protein Kinase C-epsilon
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Protein Structure
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Secondary
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Protein Structure
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Tertiary
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Spectrophotometry
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Infrared
Biuppslag (personer, institutioner, konferenser, titlar ...)
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Berglin, Mattias,1970Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xbemat
(författare)
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Elwing, Hans-Björne,1946Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xelwha
(författare)
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Egea-Jiménez, A. L.
(författare)
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Corbalán-García, S.
(författare)
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Gómez-Fernández, J. C.
(författare)
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Göteborgs universitetInstitutionen för kemi och molekylärbiologi
(creator_code:org_t)
Sammanhörande titlar
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Ingår i:Biochimica et Biophysica Acta - Biomembranes: Elsevier BV1828:2, s. 552-5600005-2736
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