2N5E

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

2N5E の概要

• エントリーDOI: 10.2210/pdb2n5e/pdb
• NMR情報: BMRB: 25710
• 分子名称: Apolipoprotein A-I (1 entity in total)
• 機能のキーワード: nanodisc, hdl, lipoproteins, cardiovascular disease, lipid binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P02647
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38923.95

構造登録者

Bibow, S.,Polyhach, Y.,Eichmann, C.,Chi, C.N.,Kowal, J.,Stahlberg, H.,Jeschke, G.,Guentert, P.,Riek, R. (登録日: 2015-07-15, 公開日: 2016-12-21, 最終更新日: 2024-05-01)

主引用文献

Bibow, 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

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

実験手法

SOLUTION NMR