Intermolecular Contact between Globular N-terminal Fold and C-terminal Domain of ApoA-I Stabilizes Its Lipid-bound Conformation
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 280, Issue: 38, Page: 33015-33025
2005
- 88Citations
- 37Captures
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Metrics Details
- Citations88
- Citation Indexes88
- 88
- CrossRef86
- Captures37
- Readers37
- 31
Article Description
The structure of apoA-I on discoidal high density lipoprotein (HDL) was studied using a combination of chemical cross-linking and mass spectrometry. Recombinant HDL particles containing 145 molecules of 1-palmitoyl-2-oleoyl- sn -glycero-3-phosphocholine and two molecules of apoA-I with a 96-Å diameter were treated with the lysine-specific cross-linker, dithiobis(succinimidylpropionate) at varying molar ratios from 2:1 to 200:1. At low molar ratios of dithiobis(succinimidylpropionate) to apoA-I, two products were obtained corresponding to ∼53 and ∼80 kDa. At high molar ratios, these two products merged, yielding a product of ∼59 kDa, close to the theoretical molecular mass of dimeric apoA-I. To identify the intermolecular cross-links giving rise to the two different sized products, bands were excised from the gel, digested with trypsin, and then analyzed by liquid chromatography-electrospray-tandem mass spectrometry. In addition, tandem mass spectrometry of unique cross-links found in the 53- and 80-kDa products suggested that a distinct conformation exists for lipid-bound apoA-I on 96-Å recombinant HDL, emphasizing the inherent flexibility and malleability of the N termini and its interaction with its C-terminal domain.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820791611; http://dx.doi.org/10.1074/jbc.m505081200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=25444491569&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/15972827; https://linkinghub.elsevier.com/retrieve/pii/S0021925820791611; http://www.jbc.org/lookup/doi/10.1074/jbc.M505081200; https://syndication.highwire.org/content/doi/10.1074/jbc.M505081200; https://dx.doi.org/10.1074/jbc.m505081200
Elsevier BV
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