Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I.

Détails

ID Serval
serval:BIB_ADBDAEFC9D46
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I.
Périodique
Nature structural & molecular biology
Auteur⸱e⸱s
Bibow S., Polyhach Y., Eichmann C., Chi C.N., Kowal J., Albiez S., McLeod R.A., Stahlberg H., Jeschke G., Güntert P., Riek R.
ISSN
1545-9985 (Electronic)
ISSN-L
1545-9985
Statut éditorial
Publié
Date de publication
02/2017
Peer-reviewed
Oui
Volume
24
Numéro
2
Pages
187-193
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
High-density lipoprotein (HDL) particles are cholesterol and lipid transport containers. Mature HDL particles destined for the liver develop through the formation of intermediate discoidal HDL particles, which are the primary acceptors for cholesterol. Here we present the three-dimensional structure of reconstituted discoidal HDL (rdHDL) particles, using a shortened construct of human apolipoprotein A-I, determined from a combination of nuclear magnetic resonance (NMR), electron paramagnetic resonance (EPR) and transmission electron microscopy (TEM) data. The rdHDL particles feature a protein double belt surrounding a lipid bilayer patch in an antiparallel fashion. The integrity of this structure is maintained by up to 28 salt bridges and a zipper-like pattern of cation-π interactions between helices 4 and 6. To accommodate a hydrophobic interior, a gross 'right-to-right' rotation of the helices after lipidation is necessary. The structure reflects the complexity required for a shuttling container to hold a fluid lipid or cholesterol interior at a protein:lipid ratio of 1:50.
Mots-clé
Apolipoprotein A-I/chemistry, Humans, Hydrophobic and Hydrophilic Interactions, Lipoproteins, HDL/chemistry, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, alpha-Helical, Protein Structure, Secondary, Solutions
Pubmed
Web of science
Création de la notice
09/06/2023 16:02
Dernière modification de la notice
08/07/2023 6:50
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