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

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: 12479569
DOI: 10.1023/A:1020566909213

Experimental method

SOLUTION NMR