Publication year
2002Source
Molecular and Cellular Biochemistry, 239, 1-2, (2002), pp. 61-8ISSN
Publication type
Article / Letter to editor

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Organization
Tumorimmunology
Biochemistry (UMC)
Journal title
Molecular and Cellular Biochemistry
Volume
vol. 239
Issue
iss. 1-2
Page start
p. 61
Page end
p. 8
Subject
Role of fatty acid-binding proteins, proteoglycans and ion transport in differentiation and pathology; De rol van vetzuurbindende eiwitten, proteoglycanen en iontransport bij differentiatie en pathologieAbstract
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.
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- Academic publications [229037]
- Faculty of Medical Sciences [87745]
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