ArticleThe Journal of biological chemistry2016
An Evaluation of the Crystal Structure of C-terminal Truncated Apolipoprotein A-I in Solution Reveals Structural Dynamics Related to Lipid Binding.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- The role of C-terminal ionic residues in self-association of apolipoprotein A-I.Biochimica et biophysica acta. Biomembranes · 2023Article
- Article
- Molecular Insights into Human Hereditary Apolipoprotein A-I Amyloidosis Caused by the Glu34Lys Mutation.Biochemistry · 2018Article
- A thumbwheel mechanism for APOA1 activation of LCAT activity in HDL.Journal of lipid research · 2018Article
- Charged Residues in the C-Terminal Domain of Apolipoprotein A-I Modulate Oligomerization.Biochemistry · 2018Article
- Characterization of homodimer interfaces with cross-linking mass spectrometry and isotopically labeled proteins.Nature protocols · 2018Article
- A consensus model of human apolipoprotein A-I in its monomeric and lipid-free state.Nature structural & molecular biology · 2017Article
- Transfer of C-terminal residues of human apolipoprotein A-I to insect apolipophorin III creates a two-domain chimeric protein with enhanced lipid binding activity.Biochimica et biophysica acta. Biomembranes · 2017Article
- Apolipoprotein A-II alters the proteome of human lipoproteins and enhances cholesterol efflux from ABCA1.Journal of lipid research · 2017Article
- High throughput quantification of apolipoproteins A-I and B-100 by isotope dilution MS targeting fast trypsin releasable peptides without reduction and alkylation.Proteomics. Clinical applications · 2017Article
- Identification of a novel lipid binding motif in apolipoprotein B by the analysis of hydrophobic cluster domains.Biochimica et biophysica acta. Biomembranes · 2017Article
- High-Density Lipoprotein Biogenesis: Defining the Domains Involved in Human Apolipoprotein A-I Lipidation.Biochemistry · 2016Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Apolipoprotein (apo) A-I mediates many of the anti-atherogenic functions attributed to high density lipoprotein. Unfortunately, efforts toward a high resolution structure of full-length apoA-I have not been fruitful, although there have been successes with deletion mutants. Recently, a C-terminal truncation (apoA-I(Δ185-243)) was crystallized as a dimer. The structure showed two helical bundles connected by a long, curved pair of swapped helical domains. To compare this structure to that existing under solution conditions, we applied small angle x-ray scattering and isotope-assisted chemical cross-linking to apoA-I(Δ185-243) in its dimeric and monomeric forms. For the dimer, we found evidence for the shared domains and aspects of the N-terminal bundles, but not the molecular curvature seen in the crystal. We also found that the N-terminal bundles equilibrate between open and closed states. Interestingly, this movement is one of the transitions proposed during lipid binding. The monomer was consistent with a model in which the long shared helix doubles back onto the helical bundle. Combined with the crystal structure, these data offer an important starting point to understand the molecular details of high density lipoprotein biogenesis.
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