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2N5E

The 3D solution structure of discoidal high-density lipoprotein particles

Summary for 2N5E
Entry DOI10.2210/pdb2n5e/pdb
NMR InformationBMRB: 25710
DescriptorApolipoprotein A-I (1 entity in total)
Functional Keywordsnanodisc, hdl, lipoproteins, cardiovascular disease, lipid binding protein
Biological sourceHomo sapiens (human)
Cellular locationSecreted: P02647
Total number of polymer chains2
Total formula weight38923.95
Authors
Bibow, S.,Polyhach, Y.,Eichmann, C.,Chi, C.N.,Kowal, J.,Stahlberg, H.,Jeschke, G.,Guentert, P.,Riek, R. (deposition date: 2015-07-15, release date: 2016-12-21, Last modification date: 2024-05-01)
Primary citationBibow, S.,Polyhach, Y.,Eichmann, C.,Chi, C.N.,Kowal, J.,Albiez, S.,McLeod, R.A.,Stahlberg, H.,Jeschke, G.,Guntert, P.,Riek, R.
Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I.
Nat.Struct.Mol.Biol., 24:187-193, 2017
Cited by
PubMed Abstract: 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.
PubMed: 28024148
DOI: 10.1038/nsmb.3345
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

數據於2024-10-30公開中

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