Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 24, Issue 2, Pages 187-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3345
Keywords
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Funding
- ETH fellowship program
- ETH Zurich
- EU COFUND program [FEL-2012-1]
- Swedish research council (Ventenskap Radet) [VR-2011-13]
- Wenner-Gren Stiftelsern [WG-13]
- NCCR TransCure
- SNF [205320_166164, 200020_157034, 144444]
- Eurostars grant - State Secretariat for Education, Research and Innovation of the Swiss Confederation [E! 9803]
- Grants-in-Aid for Scientific Research [17K07312] Funding Source: KAKEN
- Swiss National Science Foundation (SNF) [205320_166164, 200020_157034] Funding Source: Swiss National Science Foundation (SNF)
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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-pi 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.
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