Structure, Topology, and Dynamics of Membrane-Inserted Polypeptides and Lipids by Solid-State NMR Spectroscopy: Investigations of the Transmembrane Domains of the DQ Beta-1 Subunit of the MHC II Receptor and of the COP I Protein p24.
fatty acyl chain order parameter
helix topology
highly specific protein-lipid interaction
solid-state NMR
sphingomyelin recognition motif
supported lipid bilayer
transmembrane dimer
Journal
Frontiers in molecular biosciences
ISSN: 2296-889X
Titre abrégé: Front Mol Biosci
Pays: Switzerland
ID NLM: 101653173
Informations de publication
Date de publication:
2019
2019
Historique:
received:
07
06
2019
accepted:
23
08
2019
entrez:
15
10
2019
pubmed:
15
10
2019
medline:
15
10
2019
Statut:
epublish
Résumé
MHC class II receptors carry important function in adaptive immunity and their malfunctioning is associated with diabetes type I, chronic inflammatory diseases and other autoimmune diseases. The protein assembles from the DQ alpha-1 and DQ beta-1 subunits where the transmembrane domains of these type I membrane proteins have been shown to be involved in homo- and heterodimer formation. Furthermore, the DQ alpha 1 chain carries a sequence motif that has been first identified in the context of p24, a protein involved in the formation of COPI vesicles of the intracellular transport machinery, to specifically interact with sphingomyelin-C18 (SM-C18). Here we investigated the membrane interactions and dynamics of DQ beta-1 in liquid crystalline POPC phospholipid bilayers by oriented
Identifiants
pubmed: 31608287
doi: 10.3389/fmolb.2019.00083
pmc: PMC6769064
doi:
Types de publication
Journal Article
Langues
eng
Pagination
83Informations de copyright
Copyright © 2019 Salnikov, Aisenbrey, Pokrandt, Brügger and Bechinger.
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