ArticleBiophysical journal2012
Solution structure and backbone dynamics of human liver fatty acid binding protein: fatty acid binding revisited.
Article in Biophysical journal, 2012. 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, 55 citations in OpenAlex.
- A high-resolution data set of fatty acid-binding protein structures. I. Dynamics of FABP4 and ligand binding.Acta crystallographica. Section D, Structural biology · 2025Article
- Drugs Form Ternary Complexes with Human Liver Fatty Acid Binding Protein 1 (FABP1) and FABP1 Binding Alters Drug Metabolism.Molecular pharmacology · 2024Article
- Drugs Form Ternary Complexes with Human Liver Fatty Acid Binding Protein (FABP1) and FABP1 Binding Alters Drug Metabolism.bioRxiv : the preprint server for biology · 2024Article
- A genetically-encoded biosensor for direct detection of perfluorooctanoic acid.Scientific reports · 2023Article
- Impact of Intracellular Lipid Binding Proteins on Endogenous and Xenobiotic Ligand Metabolism and Disposition.Drug metabolism and disposition: the biological fate of chemicals · 2023Review
- Effects of ligand binding on dynamics of fatty acid binding protein and interactions with membranes.Biophysical journal · 2022Article
- Structural and Dynamic Determinants of Molecular Recognition in Bile Acid-Binding Proteins.International journal of molecular sciences · 2022Review
- Atomistic Insights into the Functional Instability of the Second Helix of Fatty Acid Binding Protein.Biophysical journal · 2019Article
- FABP1 controls hepatic transport and biotransformation of ΔScientific reports · 2019Article
- A ligand-induced structural change in fatty acid-binding protein 1 is associated with potentiation of peroxisome proliferator-activated receptor α agonists.The Journal of biological chemistry · 2019Article
- Different modes of barrel opening suggest a complex pathway of ligand binding in human gastrotropin.PloS one · 2019Article
- Protocols and pitfalls in obtaining fatty acid-binding proteins for biophysical studies of ligand-protein and protein-protein interactions.Biochemistry and biophysics reports · 2017Article
- Review
- CD36 binds oxidized low density lipoprotein (LDL) in a mechanism dependent upon fatty acid binding.The Journal of biological chemistry · 2015Article
- Energy landscapes of functional proteins are inherently risky.Nature chemical biology · 2014Article
- Human FABP1 T94A variant impacts fatty acid metabolism and PPAR-α activation in cultured human female hepatocytes.American journal of physiology. Gastrointestinal and liver physiology · 2014Article
- Structural and functional interaction of fatty acids with human liver fatty acid-binding protein (L-FABP) T94A variant.The FEBS journal · 2014Article
- Binding of a fluorescence reporter and a ligand to an odorant-binding protein of the yellow fever mosquito, Aedes aegypti.F1000Research · 2014Article
- Atomic resolution view into the structure-function relationships of the human myelin peripheral membrane protein P2.Acta crystallographica. Section D, Biological crystallography · 2014Article
- The human liver fatty acid binding protein T94A variant alters the structure, stability, and interaction with fibrates.Biochemistry · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Liver fatty acid binding protein (L-FABP), a cytosolic protein most abundant in liver, is associated with intracellular transport of fatty acids, nuclear signaling, and regulation of intracellular lipolysis. Among the members of the intracellular lipid binding protein family, L-FABP is of particular interest as it can i), bind two fatty acid molecules simultaneously and ii), accommodate a variety of bulkier physiological ligands such as bilirubin and fatty acyl CoA. To better understand the promiscuous binding and transport properties of L-FABP, we investigated structure and dynamics of human L-FABP with and without bound ligands by means of heteronuclear NMR. The overall conformation of human L-FABP shows the typical β-clam motif. Binding of two oleic acid (OA) molecules does not alter the protein conformation substantially, but perturbs the chemical shift of certain backbone and side-chain protons that are involved in OA binding according to the structure of the human L-FABP/OA complex. Comparison of the human apo and holo L-FABP structures revealed no evidence for an "open-cap" conformation or a "swivel-back" mechanism of the K90 side chain upon ligand binding, as proposed for rat L-FABP. Instead, we postulate that the lipid binding process in L-FABP is associated with backbone dynamics.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.