Human brain-type fatty acid-binding protein (B-FABP) has been recombinantly expressed in Escherichia coli both unlabelled and N-15-enriched for structure investigation in solution using high-resolution NMR spectroscopy. The sequential assignments of the H-1 and N-15 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 of ten 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 [ 12] 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.
CITATION STYLE
Rademacher, M., Zimmerman, A. W., Rüterjans, H., Veerkamp, J. H., & Lücke, C. (2002). Solution structure of fatty acid-binding protein from human brain. In Cellular Lipid Binding Proteins (pp. 61–68). Springer US. https://doi.org/10.1007/978-1-4419-9270-3_8
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