Predicting the structure of apolipoprotein A-I in reconstituted high-density lipoprotein disks |
| |
Authors: | JC Phillips W Wriggers Z Li A Jonas K Schulten |
| |
Affiliation: | Theoretical Biophysics, Beckman Institute and Department of Physics, College of Medicine at Urbana-Champaign, University of Illinois, Urbana 61801, USA. |
| |
Abstract: | In reconstituted high-density lipoproteins, apolipoprotein A-I and phosphatidylcholines combine to form disks in which the amphipathic alpha-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-A 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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|