ArticleActa crystallographica. Section D, Structural biology2025
A high-resolution data set of fatty acid-binding protein structures. I. Dynamics of FABP4 and ligand binding.
Article in Acta crystallographica. Section D, Structural biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Avoiding pitfalls when modelling ligands in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2026Article
- Developments and challenges in hit progression within fragment-based drug discovery.Nature communications · 2026Review
- Natural Bioactive Compounds Targeting FABP4 in Adipogenesis and Obesity: Evidence from In Vitro and In Vivo Studies.International journal of molecular sciences · 2026Review
- Molecular mechanisms underlying fetal bovine serum-induced developmental delay in mouse embryos: a data-independent acquisition (DIA)-based proteomics study.Frontiers in molecular biosciences · 2026Article
- A high-resolution data set of fatty acid-binding protein structures. III. Unexpectedly high occurrence of wrong ligands.Acta crystallographica. Section D, Structural biology · 2025Article
- A high-resolution data set of fatty acid-binding protein structures. II. Crystallographic overview, ligand classes and binding pose.Acta crystallographica. Section D, Structural biology · 2025Article
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Authors and funding
6 authors.
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Abstract
Fatty acid-binding proteins (FABPs) are involved in the uptake and intracellular trafficking of fatty acids for metabolic and gene-regulatory purposes. FABPs are known to associate with membranes and also enter the nucleus. Using NMR and a human FABP4 (hFABP4) preparation completely free of endogenous ligands, we studied the influence of fatty acids and inhibitors on the conformational flexibility and bicelle/membrane association of this isoform. Binding of fatty acids and ligands rigidifies hFABP4, particularly at the portal region where ligands enter the binding site. Depending on the nature of the ligand, hFABP4 stays associated with bicelles via the portal region or segregates into solution, a prerequisite for nuclear import using a nonclassical nuclear localization signal. These results indicate that different ligands can lead to different biological outcomes. One of the major determinants for FABP4 segregation is Phe58, which in X-ray crystal structures adopts different conformations as a function of ligand volume. It is possible that other FABP isoforms use a similar mechanism for ligand-dependent membrane detachment and activation of nuclear import.
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