Apolipophorin III (apoLp-III) is an exchangeable apolipoprotein found in insects and plays an important function in lipid transport. The protein has an unusual five-helix bundle architecture, deviating from the common four-helix bundle motif. To understand the role of the additional helix in apoLp-III, the N-terminal or C-terminal helix was deleted to create a putative four-helix bundle protein. While the protein lacking helix-1 could be expressed in bacteria albeit at reduced yields, apoLp-III lacking helix-5 could not be produced. Mutational analysis by truncating helix-5 showed that a minimum segment of approximately one-third of the C-terminal helix is required for protein expression. The variant lacking helix-5 was produced by inserting a methionine residue between helix-4 and -5; subsequent cyanogenbromide cleavage generated the four-helix variant. Both N- and C-terminal helix deletion variants displayed significantly reduced helical content, protein stability, and tertiary structure. Despite the significantly altered structure, the variants were still fully functional. The rate of dimyristoylphosphatidylcholine vesicle solubilization was enhanced 4-5-fold compared to the wild-type protein, and the deletion variants were ...Continue Reading
Different isoforms of an apoprotein (apolipophorin III) associate with lipoproteins in Locusta migratoria
Immunocytochemical localization of lipophorins in the flight muscles of the migratory locust (Locusta migratoria) at rest and during flight
Spectroscopic and lipid binding studies on the amino and carboxyl terminal fragments of Locusta migratoria apolipophorin III
Alignment of the apolipophorin-III alpha-helices in complex with dimyristoylphosphatidylcholine. A unique spatial orientation.
Structural and binding characteristics of the carboxyl terminal fragment of apolipophorin III from Manduca sexta
Prevention of phospholipase-C induced aggregation of low density lipoprotein by amphipathic apolipoproteins
Disulfide bond engineering to monitor conformational opening of apolipophorin III during lipid binding.
Insight into lipid surface recognition and reversible conformational adaptations of an exchangeable apolipoprotein by multidimensional heteronuclear NMR techniques.
Interhelical contacts are required for the helix bundle fold of apolipophorin III and its ability to interact with lipoproteins
The lipid binding activity of the exchangeable apolipoprotein apolipophorin-III correlates with the formation of a partially folded conformation
Lipid binding of the exchangeable apolipoprotein apolipophorin III induces major changes in fluorescence properties of tryptophans 115 and 130
Differences in stability among the human apolipoprotein E isoforms determined by the amino-terminal domain
An N-terminal three-helix fragment of the exchangeable insect apolipoprotein apolipophorin III conserves the lipid binding properties of wild-type protein
Conformational changes of an exchangeable apolipoprotein, apolipophorin III from Locusta migratoria, at low pH: correlation with lipid binding
Essential role of the conformational flexibility of helices 1 and 5 on the lipid binding activity of apolipophorin-III
Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein
Structure of apolipophorin-III in discoidal lipoproteins. Interhelical distances in the lipid-bound state and conformational change upon binding to lipid
Lipid-triggered conformational switch of apolipophorin III helix bundle to an extended helix organization
Influence of apoE domain structure and polymorphism on the kinetics of phospholipid vesicle solubilization.
NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III.
Lipid binding ability of human apolipoprotein E N-terminal domain isoforms: correlation with protein stability?
Role of buried polar residues in helix bundle stability and lipid binding of apolipophorin III: destabilization by threonine 31
Crystal structure of C-terminal truncated apolipoprotein A-I reveals the assembly of high density lipoprotein (HDL) by dimerization.
Impact of statin use on cancer-specific mortality and recurrence: A meta-analysis of 60 observational studies
Structural and Functional Characterisation of the Domains of Ubiquitin-Activating Enzyme (E1) of Saccharomyces cerevisiae.
Vitamin E Derivative with Modified Side Chain Induced Apoptosis by Modulating the Cellular Lipids and Membrane Dynamics in MCF7 Cells
The membrane protein KCNQ1 potassium ion channel: Functional diversity and current structural insights
A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins.
Terminal Peptide Extensions Augment the Retinal IMPDH1 Catalytic Activity and Attenuate the ATP-induced Fibrillation Events.
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