ArticleThe Journal of biological chemistry2009
Fatty acid- and retinoid-binding proteins have distinct binding pockets for the two types of cargo.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 54 citations in OpenAlex.
- Characterization and ligand binding properties of a fatty acid- and retinol- binding protein (Hp-FAR-2) from Heligmosomoides polygyrus.PLoS neglected tropical diseases · 2025Article
- A secreted fatty acid- and retinol- binding protein frombioRxiv : the preprint server for biology · 2025Article
- Nb-FAR-1: A key developmental protein affects lipid droplet accumulation and cuticle formation in Nippostrongylus brasiliensis.PLoS neglected tropical diseases · 2025Article
- Proteomic characterization and comparison of the infective and adult life stage secretomes from Necator americanus and Ancylostoma ceylanicum.PLoS neglected tropical diseases · 2025Article
- Fatty acid- and retinol-binding protein 6 does not control worm fatty acid content in Caenorhabditis elegans but might play a role in Haemonchus contortus parasitism.Parasites & vectors · 2023Article
- The FAR protein family of parasitic nematodes.PLoS pathogens · 2022Review
- Function of lipid binding proteins of parasitic helminths: still a long road.Parasitology research · 2022Review
- Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways.PLoS pathogens · 2021Article
- Mining nematode protein secretomes to explain lifestyle and host specificity.PLoS neglected tropical diseases · 2021Article
- Genus-level evolutionary relationships of FAR proteins reflect the diversity of lifestyles of free-living and parasitic nematodes.BMC biology · 2021Article
- Ligand binding properties of two Brugia malayi fatty acid and retinol (FAR) binding proteins and their vaccine efficacies against challenge infection in gerbils.PLoS neglected tropical diseases · 2018Article
- Describing the Diapause-Preparatory Proteome of the BeetleFrontiers in physiology · 2017Article
- Article
- Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus.The Biochemical journal · 2015Article
- Article
- The structure and dynamics of BmR1 protein from Brugia malayi: in silico approaches.International journal of molecular sciences · 2014Article
- ¹H, ¹³C and ¹⁵N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus.Biomolecular NMR assignments · 2014Article
- Two crystal forms of a helix-rich fatty acid- and retinol-binding protein, Na-FAR-1, from the parasitic nematode Necator americanus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Structural and binding properties of two paralogous fatty acid binding proteins of Taenia solium metacestode.PLoS neglected tropical diseases · 2012Article
- Solution structure of a repeated unit of the ABA-1 nematode polyprotein allergen of Ascaris reveals a novel fold and two discrete lipid-binding sites.PLoS neglected tropical diseases · 2011Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Parasitic nematodes cause serious diseases in humans, animals, and plants. They have limited lipid metabolism and are reliant on lipid-binding proteins to acquire these metabolites from their hosts. Several structurally novel families of lipid-binding proteins in nematodes have been described, including the fatty acid- and retinoid-binding protein family (FAR). In Caenorhabditis elegans, used as a model for studying parasitic nematodes, eight C. elegans FAR proteins have been described. The crystal structure of C. elegans FAR-7 is the first structure of a FAR protein, and it exhibits a novel fold. It differs radically from the mammalian fatty acid-binding proteins and has two ligand binding pockets joined by a surface groove. The first can accommodate the aliphatic chain of fatty acids, whereas the second can accommodate the bulkier retinoids. In addition to demonstrating lipid binding by fluorescence spectroscopy, we present evidence that retinol binding is positively regulated by casein kinase II phosphorylation at a conserved site near the bottom of the second pocket. far-7::GFP (green fluorescent protein) expression shows that it is localized in the head hypodermal syncytia and the excretory cell but that this localization changes under starvation conditions. In conclusion, our study provides the basic structural and functional information for investigation of inhibitors of lipid binding by FAR proteins.
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