Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Mol Biol. 2011 Jan 7;405(1):274-83. doi: 10.1016/j.jmb.2010.10.034. Epub 2010 Oct 26.

Enhancing the contrast of ApoB to locate the surface components in the 3D density map of human LDL.

Author information

  • 1Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118, USA.

Abstract

A 26 Å resolution map of the structure of human low-density lipoprotein (LDL) was obtained from electron cryomicroscopy and single-particle image reconstruction. The structure showed a discoidal-shaped LDL particle with high-density regions mainly distributed at the edge of the particle and low-density regions at the flat surface that covers the core region. To determine the chemical components that correspond to these density regions and to delineate the distribution of protein and phospholipid located at the particle surface at the resolution of the map, we used Mono-Sulfo-NHS-Undecagold labeling to increase preferentially the contrast of the apolipoprotein B component on the LDL particle. In the three-dimensional map from the image reconstruction of the undecagold-labeled LDL particles, the high-density region from the undecagold label was distributed mainly at the edge of the particle, and lower density regions were found at the flat surfaces that cover the neutral lipid core. This suggests that apolipoprotein B mainly encircles LDL at the edge of the particle and the phospholipid monolayers are located at the flat surfaces, which are parallel to the cholesterol ester layers in the core and may interact with the core lipid layers through the acyl chains.

Copyright © 2010 Elsevier Ltd. All rights reserved.

PMID:
21029740
[PubMed - indexed for MEDLINE]
PMCID:
PMC3006490
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Write to the Help Desk