ArticleBiophysical journal2006
Fatty acid binding proteins: same structure but different binding mechanisms? Molecular dynamics simulations of intestinal fatty acid binding protein.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 50 citations in OpenAlex.
- Functional thermodynamics govern the ligand binding to human cytosolic transport proteins.Protein science : a publication of the Protein Society · 2026Article
- Fatty acid binding to the human transport proteins FABP3, FABP4, and FABP5 from a Ligand's perspective.The Journal of biological chemistry · 2024Article
- Review
- Atomistic Insights into the Functional Instability of the Second Helix of Fatty Acid Binding Protein.Biophysical journal · 2019Article
- The Observation of Ligand-Binding-Relevant Open States of Fatty Acid Binding Protein by Molecular Dynamics Simulations and a Markov State Model.International journal of molecular sciences · 2019Article
- Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the β barrel in fatty acid binding proteins.BMC structural biology · 2018Article
- Conformational Flexibility Differentiates Naturally Occurring Bet v 1 Isoforms.International journal of molecular sciences · 2017Article
- Concerted dynamic motions of an FABP4 model and its ligands revealed by microsecond molecular dynamics simulations.Biochemistry · 2014Article
- Crystallographic study of FABP5 as an intracellular endocannabinoid transporter.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Article
- Insight into the interaction sites between fatty acid binding proteins and their ligands.Journal of molecular modeling · 2010Article
- Molecular dynamics simulation of ligand dissociation from liver fatty acid binding protein.PloS one · 2009Article
- Buffer interference with protein dynamics: a case study on human liver fatty acid binding protein.Biophysical journal · 2009Article
- Modeling fatty acid delivery from intestinal fatty acid binding protein to a membrane.Protein science : a publication of the Protein Society · 2007Article
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Authors and funding
3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Fatty acid binding proteins (FABPs) carry fatty acids (FAs) and other lipids in the cellular environment, and are thus involved in processes such as FA uptake, transport, and oxidation. These proteins bind either one or two ligands in a binding site, which appears to be inaccessible from the bulk. Thus, the entry of the substrate necessitates a conformational change, whose nature is still unknown. A possible description of the ligand binding process is given by the portal hypothesis, which suggests that the FA enters the protein through a dynamic area known as the portal region. On the other hand, recent simulations of the adipocyte lipid binding protein (ALBP) suggested a different entry site (the alternative portal). In this article, we discuss molecular dynamics simulations of the apo-intestinal-FABP (I-FABP) in the presence of palmitate molecule(s) in the simulation box. The simulations were carried out to study whether the FA can enter the protein during the simulations (as in the ALBP) and where the ligand entry site is (the portal region, the alternative portal or a different domain). The analysis of the simulations revealed a clear difference between the ALBP and the I-FABP. In the latter case, the palmitate preferentially adsorbed to the portal region, which was more mobile than the rest of the protein. However, no ligand entry was observed in the multi-nanosecond-long simulations, in contrast to ALBP. These findings suggest that, although the main structural motif of the FABPs is common, the fine details of each individual protein structure grossly modulate its reactivity.
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