ArticleProtein science : a publication of the Protein Society2007
Modeling fatty acid delivery from intestinal fatty acid binding protein to a membrane.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 25 citations in OpenAlex.
- Mechanism of negative membrane curvature generation by I-BAR domains.Structure (London, England : 1993) · 2021Article
- Probing the interaction of brain fatty acid binding protein (B-FABP) with model membranes.PloS one · 2013Article
- Millisecond timescale dynamics of human liver fatty acid binding protein: testing of its relevance to the ligand entry process.Biophysical journal · 2010Article
- 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
- Molecular dynamics study of the interaction between fatty acid binding proteins with palmitate mini-micelles.Molecular and cellular biochemistry · 2009Article
- Interaction of enterocyte FABPs with phospholipid membranes: clues for specific physiological roles.Biochimica et biophysica actaArticle
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Intestinal fatty acid binding protein (IFABP) interacts with biological membranes and delivers fatty acid (FA) into them via a collisional mechanism. However, the membrane-bound structure of the protein and the pathway of FA transfer are not precisely known. We used molecular dynamics (MD) simulations with an implicit membrane model to determine the optimal orientation of apo- and holo-IFABP (bound with palmitate) on an anionic membrane. In this orientation, the helical portal region, delimited by the alphaII helix and the betaC-betaD and betaE-betaF turns, is oriented toward the membrane whereas the putative beta-strand portal, delimited by the betaB-betaC, betaF-betaG, betaH-betaI turns and the N terminus, is exposed to solvent. Starting from the MD structure of holo-IFABP in the optimal orientation relative to the membrane, we examined the release of palmitate via both pathways. Although the domains can widen enough to allow the passage of palmitate, fatty acid release through the helical portal region incurs smaller conformational changes and a lower energetic cost.
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Registered trials
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.