ArticleBiochemistry2009
Interaction between the N- and C-terminal domains modulates the stability and lipid binding of apolipoprotein A-I.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Mannose-functionalization of reconstituted high-density lipoprotein nanoparticles improves payload delivery and enhances M2-to-M1 phenotype reprogramming of RAW 264.7 macrophages polarized by B16-F10 melanoma cells.Frontiers in drug delivery · 2023Article
- Site-specific 5-hydroxytryptophan incorporation into apolipoprotein A-I impairs cholesterol efflux activity and high-density lipoprotein biogenesis.The Journal of biological chemistry · 2020Article
- First eight residues of apolipoprotein A-I mediate the C-terminus control of helical bundle unfolding and its lipidation.PloS one · 2020Article
- Effect of Phosphatidylserine and Cholesterol on Membrane-mediated Fibril Formation by the N-terminal Amyloidogenic Fragment of Apolipoprotein A-I.Scientific reports · 2018Article
- Characterization of type IV antifreeze gene in Nile tilapia (Oreochromis niloticus) and influence of cold and hot weather on its expression and some immune-related genes.Fish physiology and biochemistry · 2018Article
- A consensus model of human apolipoprotein A-I in its monomeric and lipid-free state.Nature structural & molecular biology · 2017Article
- High-Density Lipoprotein Biogenesis: Defining the Domains Involved in Human Apolipoprotein A-I Lipidation.Biochemistry · 2016Article
- Structural Stability and Local Dynamics in Disease-Causing Mutants of Human Apolipoprotein A-I: What Makes the Protein Amyloidogenic?Journal of molecular biology · 2016Article
- Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.The Journal of biological chemistry · 2015Article
- A model of lipid-free apolipoprotein A-I revealed by iterative molecular dynamics simulation.PloS one · 2015Article
- Fluorescence study of domain structure and lipid interaction of human apolipoproteins E3 and E4.Biochimica et biophysica acta · 2014Article
- Influence of domain stability on the properties of human apolipoprotein E3 and E4 and mouse apolipoprotein E.Biochemistry · 2014Article
- The roles of C-terminal helices of human apolipoprotein A-I in formation of high-density lipoprotein particles.Biochimica et biophysica acta · 2014Article
- New insights into the determination of HDL structure by apolipoproteins: Thematic review series: high density lipoprotein structure, function, and metabolism.Journal of lipid research · 2013Review
- Interactions of apolipoprotein A-I with high-density lipoprotein particles.Biochemistry · 2013Article
- Crystal structure of Δ(185-243)ApoA-I suggests a mechanistic framework for the protein adaptation to the changing lipid load in good cholesterol: from flatland to sphereland via double belt, belt buckle, double hairpin and trefoil/tetrafoil.Journal of molecular biology · 2013Article
- Fluorescence analysis of the lipid binding-induced conformational change of apolipoprotein E4.Biochemistry · 2012Article
- Naturally occurring variant of mouse apolipoprotein A-I alters the lipid and HDL association properties of the protein.Journal of lipid research · 2012Article
- Influence of C-terminal α-helix hydrophobicity and aromatic amino acid content on apolipoprotein A-I functionality.Biochimica et biophysica acta · 2012Article
- The "beta-clasp" model of apolipoprotein A-I--a lipid-free solution structure determined by electron paramagnetic resonance spectroscopy.Biochimica et biophysica acta · 2012Article
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Authors and funding
6 authors.
Funding
Abstract
The tertiary structures of human and mouse apolipoprotein A-I (apoA-I) are comprised of an N-terminal helix bundle and a separate C-terminal domain. To define the possible intramolecular interaction between the N- and the C-terminal domains, we examined the effects on protein stability and lipid-binding properties of exchanging either the C-terminal domain or helix between human and mouse apoA-I. Chemical denaturation experiments demonstrated that replacement of the C-terminal domain or helical segment in human apoA-I with the mouse counterparts largely destabilizes the N-terminal helix bundle. Removal of the C-terminal domain or alpha-helix in human apoA-I had a similar effect on the destabilization of the helix bundle against urea denaturation, indicating that the C-terminal helical segment mainly contributes to stabilizing the N-terminal helix bundle structure in the apoA-I molecule. Consistent with this, KI quenching experiments indicated that removal or replacement of the C-terminal domain or helix in human apoA-I causes Trp residues in the N-terminal domain to become exposed to solvent. Measurements of the heats of binding to egg phosphatidylcholine (PC) vesicles and the kinetics of solubilization of dimyristoyl PC vesicles demonstrated that the destabilized human N-terminal helix bundle can strongly interact with lipids without the hydrophobic C-terminal helix. In addition, site-specific labeling of the N- and C-terminal helices by acrylodan to probe the conformational stability and the spatial proximity of the two domains indicated that the C-terminal helix is located near the N-terminal helix bundle, leading to a relatively less solvent-exposed, more organized conformation of the C-terminal domain. Taken together, these results suggest that interaction between the N- and C-terminal tertiary structure domains in apoA-I modulates the stability and lipid-binding properties of the N-terminal helix bundle.
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