A model of lipid-free Apolipoprotein A-I revealed by iterative molecular dynamics simulation
Abstract
Apolipoprotein A-I (apo A-I), the major protein component of high-density lipoprotein, has been proven inversely correlated to cardiovascular risk in past decades. The lipid-free state of apo A-I is the initial stage which binds to lipids forming high-density lipoprotein. Molecular models of lipid-free apo A-I have been reported by methods like X-ray crystallography and chemical cross-linking/mass spectrometry (CCL/MS). Through structural analysis we found that those current models had limited consistency with other experimental results, such as those from hydrogen exchange with mass spectrometry. Through molecular dynamics simulations, we also found those models could not reach a stable equilibrium state. Therefore, by integrating various experimental results, we proposed a new structural model for lipidfree apo A-I, which contains a bundled four-helix N-terminal domain (1–192) that forms a variable hydrophobic groove and a mobile short hairpin C-terminal domain (193–243). This model exhibits an equilibrium state through molecular dynamics simulation and is consistent with most of the experimental results known from CCL/MS on lysine pairs, fluorescence resonance energy transfer and hydrogen exchange. This solution-state lipid-free apo A-I model may elucidate the possible conformational transitions of apo A-I binding with lipids in high-density lipoprotein formation.
- Authors:
-
- Xi'an Jiaotong Univ., Xi'an, Shaanxi (People's Republic of China); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
- Xi'an Jiaotong Univ., Xi'an, Shaanxi (People's Republic of China)
- Publication Date:
- Research Org.:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1190954
- Grant/Contract Number:
- AC02-05CH11231
- Resource Type:
- Accepted Manuscript
- Journal Name:
- PLoS ONE
- Additional Journal Information:
- Journal Volume: 10; Journal Issue: 3; Journal ID: ISSN 1932-6203
- Publisher:
- Public Library of Science
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Zhang, Xing, Lei, Dongsheng, Zhang, Lei, Rames, Matthew, and Zhang, Shengli. A model of lipid-free Apolipoprotein A-I revealed by iterative molecular dynamics simulation. United States: N. p., 2015.
Web. doi:10.1371/journal.pone.0120233.
Zhang, Xing, Lei, Dongsheng, Zhang, Lei, Rames, Matthew, & Zhang, Shengli. A model of lipid-free Apolipoprotein A-I revealed by iterative molecular dynamics simulation. United States. https://doi.org/10.1371/journal.pone.0120233
Zhang, Xing, Lei, Dongsheng, Zhang, Lei, Rames, Matthew, and Zhang, Shengli. Fri .
"A model of lipid-free Apolipoprotein A-I revealed by iterative molecular dynamics simulation". United States. https://doi.org/10.1371/journal.pone.0120233. https://www.osti.gov/servlets/purl/1190954.
@article{osti_1190954,
title = {A model of lipid-free Apolipoprotein A-I revealed by iterative molecular dynamics simulation},
author = {Zhang, Xing and Lei, Dongsheng and Zhang, Lei and Rames, Matthew and Zhang, Shengli},
abstractNote = {Apolipoprotein A-I (apo A-I), the major protein component of high-density lipoprotein, has been proven inversely correlated to cardiovascular risk in past decades. The lipid-free state of apo A-I is the initial stage which binds to lipids forming high-density lipoprotein. Molecular models of lipid-free apo A-I have been reported by methods like X-ray crystallography and chemical cross-linking/mass spectrometry (CCL/MS). Through structural analysis we found that those current models had limited consistency with other experimental results, such as those from hydrogen exchange with mass spectrometry. Through molecular dynamics simulations, we also found those models could not reach a stable equilibrium state. Therefore, by integrating various experimental results, we proposed a new structural model for lipidfree apo A-I, which contains a bundled four-helix N-terminal domain (1–192) that forms a variable hydrophobic groove and a mobile short hairpin C-terminal domain (193–243). This model exhibits an equilibrium state through molecular dynamics simulation and is consistent with most of the experimental results known from CCL/MS on lysine pairs, fluorescence resonance energy transfer and hydrogen exchange. This solution-state lipid-free apo A-I model may elucidate the possible conformational transitions of apo A-I binding with lipids in high-density lipoprotein formation.},
doi = {10.1371/journal.pone.0120233},
journal = {PLoS ONE},
number = 3,
volume = 10,
place = {United States},
year = {Fri Mar 20 00:00:00 EDT 2015},
month = {Fri Mar 20 00:00:00 EDT 2015}
}
Web of Science
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Works referencing / citing this record:
Lipidated apolipoprotein E4 structure and its receptor binding mechanism determined by a combined cross-linking coupled to mass spectrometry and molecular dynamics approach
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