Predicting the structure of apolipoprotein A-I in reconstituted high- density lipoprotein disks

James C. Phillips, Willy Wriggers, Zhigang Li, Ana Jonas, Klaus Schulten

Research output: Contribution to journalArticle

Abstract

In reconstituted high-density lipoproteins, apolipoprotein A-I and phosphatidylcholines combine to form disks in which the amphipathic α- helices of apolipoprotein A-1 bind to the edge of a lipid bilayer core, shielding the hydrophic lipid tails from the aqueous environment. We have employed experimental data, sequence analysis, and molecular modeling to construct an atomic model of such a reconstituted high-density lipoprotein disk consisting of two apolipoprotein A-I proteins and 160 palmitoyloleoylphosphatidylcholine lipids. The initial globular domain (1- 47) of apolipoprotein A-I was excluded from the model, which was hydrated with an 8-Å shell of water molecules. Molecular dynamics and simulated annealing were used to test the stability of the model. Both head-to-tail and head-to-head forms of a reconstituted high-density lipoprotein were simulated. In our simulations the protein contained and adhered to the lipid bilayer while providing good coverage of the lipid tails.

Original languageEnglish (US)
Pages (from-to)2337-2346
Number of pages10
JournalBiophysical journal
Volume73
Issue number5
DOIs
StatePublished - 1997

ASJC Scopus subject areas

  • Biophysics

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