http://www.cnr.it/ontology/cnr/individuo/prodotto/ID273760
Ligand Binding Promiscuity of Human Liver Fatty Acid Binding Protein: Structural and Dynamic Insights from an Interaction Study with Glycocholate and Oleate (Articolo in rivista)
- Type
- Label
- Ligand Binding Promiscuity of Human Liver Fatty Acid Binding Protein: Structural and Dynamic Insights from an Interaction Study with Glycocholate and Oleate (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/cbic.201300156 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Favretto F.; Assfalg M.; Gallo M.; Cicero D.O.; D'Onofrio M.;Molinari H. (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- D'Onofrio, M (Reprint Author), Univ Verona, NMR Lab, Dept Biotechnol, Str Grazie 15, I-37134 Verona, Italy. Favretto, Filippo; Assfalg, Michael; D'Onofrio, Mariapina, Univ Verona, NMR Lab, Dept Biotechnol, I-37134 Verona, Italy. Gallo, Mariana, Consejo Nacl Invest Cient & Tecn, Fdn Inst Leloir, IIBBA, RA-1033 Buenos Aires, DF, Argentina. Cicero, Daniel Oscar, Univ Roma Tor Vergata, Dept Chem Sci & Technol, I-00133 Rome, Italy. Molinari, Henriette, ISMAC CNR, Lab NMR, I-20133 Milan, Italy. (literal)
- Titolo
- Ligand Binding Promiscuity of Human Liver Fatty Acid Binding Protein: Structural and Dynamic Insights from an Interaction Study with Glycocholate and Oleate (literal)
- Abstract
- Human liver fatty acid binding protein (hL-FABP) has been reported to act as an intracellular shuttle of lipid molecules, thus playing a central role in systemic metabolic homeostasis. The involvement of hL-FABP in the transport of bile salts has been postulated but scarcely investigated. Here we describe a thorough NMR investigation of glycocholate (GCA) binding to hL-FABP. The protein molecule bound a single molecule of GCA, in contrast to the 1: 2 stoichiometry observed with fatty acids. GCA was found to occupy the large internal cavity of hL-FABP, without requiring major conformational rearrangement of the protein backbone; rather, this led to increased stability, similar to that estimated for the hL-FABP: oleate complex. Fast-timescale dynamics appeared not to be significantly perturbed in the presence of ligands. Slow motions (unlike for other proteins of the family) were retained or enhanced upon binding, consistent with a requirement for structural plasticity for promiscuous recognition. (literal)
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