1JJX
Solution Structure of Recombinant Human Brain-type Fatty acid Binding Protein
Summary for 1JJX
| Entry DOI | 10.2210/pdb1jjx/pdb |
| Related | 1FDQ |
| NMR Information | BMRB: 5320 |
| Descriptor | BRAIN-TYPE FATTY ACID BINDING PROTEIN (1 entity in total) |
| Functional Keywords | beta barrel, lipid binding protein, fatty acid carrier, 15n isotope enrichment, nmr spectroscopy |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: O15540 |
| Total number of polymer chains | 1 |
| Total formula weight | 14776.70 |
| Authors | Rademacher, M.,Zimmerman, A.W.,Rueterjans, H.,Veerkamp, J.H.,Luecke, C. (deposition date: 2001-07-10, release date: 2002-10-30, Last modification date: 2024-05-22) |
| Primary citation | Rademacher, M.,Zimmerman, A.W.,Ruterjans, H.,Veerkamp, J.H.,Lucke, C. Solution structure of fatty acid-binding protein from human brain. Mol.Cell.Biochem., 239:61-68, 2002 Cited by PubMed 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. PubMed: 12479569DOI: 10.1023/A:1020566909213 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
