ArticleMolecular and cellular biochemistry2002
Solution structure of fatty acid-binding protein from human brain.
Article in Molecular and cellular biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Fatty acid-binding proteins 3, 7, and 8 bind cholesterol and facilitate its egress from lysosomes.The Journal of cell biology · 2024Article
- Molecular Basis for the Selectivity of DHA and EPA in Sudlow's Drug Binding Sites in Human Serum Albumin with the Combined Use of NMR and Docking Calculations.Molecules (Basel, Switzerland) · 2023Article
- A combined computational-biophysical approach to understanding fatty acid binding to FABP7.Biophysical journal · 2023Article
- Understanding FABP7 binding to fatty acid micelles and membranes.Biophysical journal · 2023Article
- Gut-inhabiting Clostridia build human GPCR ligands by conjugating neurotransmitters with diet- and human-derived fatty acids.Nature microbiology · 2021Article
- Fatty Acid Signaling Mechanisms in Neural Cells: Fatty Acid Receptors.Frontiers in cellular neuroscience · 2019Review
- Hydrogen-bonded His93 as a sensitive probe for identifying inhibitors of the endocannabinoid transport protein FABP7.Chemical biology & drug design · 2015Article
- Probing the interaction of brain fatty acid binding protein (B-FABP) with model membranes.PloS one · 2013Article
- New insights on the protein-ligand interaction differences between the two primary cellular retinol carriers.Journal of lipid research · 2010Article
- New technologies for drug delivery across the blood brain barrier.Current pharmaceutical design · 2004Review
- New insights into intracellular lipid binding proteins: The role of buried water.Protein science : a publication of the Protein Society · 2002Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human brain-type fatty acid-binding protein (B-FABP) has been recombinantly expressed in Escherichia coli both unlabelled and 15N-enriched for structure investigation in solution using high-resolution NMR spectroscopy. The sequential assignments of the 1H and 15N resonances were achieved by applying multidimensional homo- and heteronuclear NMR experiments. The ensemble of the 20 final energy-minimized structures, representing human B-FABP in solution, have been calculated based on a total of 2490 meaningful distance constraints. The overall B-FABP structure exhibits the typical backbone conformation described for other members of the FABP family, consisting often antiparallel beta-strands (betaA to betaJ) that form two almost orthogonal beta-sheets, a helix-turn-helix motif that closes the beta-barrel on one side, and a short N-terminal helical loop. A comparison with the crystal structure of the same protein complexed with docosahexaenoic acid reveals only minor differences in both secondary structure and overall topology. Moreover, the NMR data indicate a close structural relationship between human B-FABP and heart-type FABP with respect to fatty acid binding inside the protein cavity.
Indexed as
Identifiers
12479569W1918445444What OpenQuestion holds
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.