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Sökning: id:"swepub:oai:gup.ub.gu.se/195351" > Membrane docking mo...

  • Ausili, A. (författare)

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

  • Artikel/kapitelEngelska2013

Förlag, utgivningsår, omfång ...

  • Elsevier BV,2013

Nummerbeteckningar

  • LIBRIS-ID:oai:gup.ub.gu.se/195351
  • https://gup.ub.gu.se/publication/195351URI
  • https://doi.org/10.1016/j.bbamem.2012.10.015DOI

Kompletterande språkuppgifter

  • Språk:engelska

Ingår i deldatabas

Klassifikation

  • Ämneskategori:ref swepub-contenttype
  • Ämneskategori:art swepub-publicationtype

Anmärkningar

  • 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

  • NATURVETENSKAP Biologi Biokemi och molekylärbiologi hsv//swe
  • NATURAL SCIENCES Biological Sciences Biochemistry and Molecular Biology hsv//eng
  • 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

Biuppslag (personer, institutioner, konferenser, titlar ...)

  • Berglin, Mattias,1970Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xbemat (författare)
  • Elwing, Hans-Björne,1946Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xelwha (författare)
  • Egea-Jiménez, A. L. (författare)
  • Corbalán-García, S. (författare)
  • Gómez-Fernández, J. C. (författare)
  • Göteborgs universitetInstitutionen för kemi och molekylärbiologi (creator_code:org_t)

Sammanhörande titlar

  • Ingår i:Biochimica et Biophysica Acta - Biomembranes: Elsevier BV1828:2, s. 552-5600005-2736

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