ArticleActa crystallographica. Section D, Structural biology2025
A high-resolution data set of fatty acid-binding protein structures. II. Crystallographic overview, ligand classes and binding pose.
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 5 papers.
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Who cites it
5 citing papers in PubMed.
- Towards routine accurate electron-density studies of biological macromolecules.Acta crystallographica. Section D, Structural biology · 2026Article
- Avoiding pitfalls when modelling ligands in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2026Article
- Radiation damage in sub-Ångström resolution macromolecular crystallography: a low-dose study.Acta crystallographica. Section D, Structural biology · 2026Article
- 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
- 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
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Authors and funding
3 authors.
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Abstract
Fatty acid-binding protein isoforms 4 and 5 are potential diabetes and atherosclerosis targets. During a drug-design program aiming at dual isoform-specific FABP4/5 inhibitors with little or no affinity for FABP3, a set of crystal structures with a median resolution of 1.2 Å was generated. The chemical space of the ligands covers various series in which the carboxylate and aliphatic groups of the natural fatty-acid ligands have been replaced by other moieties. A summary of binding modes of the chemical series is also given with respect to how isoform specificity was achieved. Additionally, several bromine-containing ligands were identified that allowed SAD phasing, yielding an independent experimental confirmation of their chemical composition.
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