1MVG
NMR solution structure of chicken Liver basic Fatty Acid Binding Protein (Lb-FABP)
Summary for 1MVG
| Entry DOI | 10.2210/pdb1mvg/pdb |
| Descriptor | Liver basic Fatty Acid Binding Protein (1 entity in total) |
| Functional Keywords | beta-barrel, calycin, ten antiparallel beta strands, helix-turn-helix motif, fatty acid binding protein, transport protein |
| Biological source | Gallus gallus (chicken) |
| Cellular location | Cytoplasm: P80226 |
| Total number of polymer chains | 1 |
| Total formula weight | 14100.18 |
| Authors | Vasile, F.,Ragona, L.,Catalano, M.,Zetta, L.,Perduca, M.,Monaco, H.,Molinari, H. (deposition date: 2002-09-25, release date: 2003-03-04, Last modification date: 2024-05-22) |
| Primary citation | Vasile, F.,Ragona, L.,Catalano, M.,Zetta, L.,Perduca, M.,Monaco, H.,Molinari, H. Solution Structure of chicken Liver basic type Fatty Acid Binding Protein J.BIOMOL.NMR, 25:157-160, 2003 Cited by PubMed 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 (1)H NMR. The overall fold of Lb-FABP, common to the other proteins of the family, consists of ten antiparallel beta-strands organised in two nearly ortogonal beta-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. PubMed: 12652125DOI: 10.1023/A:1022277727303 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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