Chicken liver basic fatty acid binding protein (Lb-FABP) belongs to the basic-type fatty acid binding proteins, a novel group of proteins isolated from liver of different non mammalian species whose structure is not known. The structure of Lb-FABP has been solved by 1H NMR. The overall fold of Lb-FABP, common to the other proteins of the family, consists of ten antiparallel β-strands organised in two nearly ortogonal β-sheets with two alpha helices closing the protein cavity where small hydrophobic ligands can be bound. The binding specificity of the protein is not known, however, based on the high sequence and structural similarity with an orthologous protein, ileal lipid binding protein, it is suggested that bile acids may be the putative ligands.

Solution structure of chicken liver basic fatty acid binding protein / F. Vasile, L. Ragona, M. Catalano, L. Zetta, M. Perduca, H. Monaco, H. Molinari. - In: JOURNAL OF BIOMOLECULAR NMR. - ISSN 0925-2738. - 25:2(2003), pp. 157-160. [10.1023/A:1022277727303]

Solution structure of chicken liver basic fatty acid binding protein

F. Vasile;
2003

Abstract

Chicken liver basic fatty acid binding protein (Lb-FABP) belongs to the basic-type fatty acid binding proteins, a novel group of proteins isolated from liver of different non mammalian species whose structure is not known. The structure of Lb-FABP has been solved by 1H NMR. The overall fold of Lb-FABP, common to the other proteins of the family, consists of ten antiparallel β-strands organised in two nearly ortogonal β-sheets with two alpha helices closing the protein cavity where small hydrophobic ligands can be bound. The binding specificity of the protein is not known, however, based on the high sequence and structural similarity with an orthologous protein, ileal lipid binding protein, it is suggested that bile acids may be the putative ligands.
calycins; chicken liver-basic FABP; NMR structure
Settore CHIM/06 - Chimica Organica
2003
Article (author)
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/721038
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