Human epidermal-type fatty acid-binding protein (E-FABP) belongs to a family of intracellular 14–15kDa lipid-binding proteins, whose functions have been associated with fatty acid signalling, cell growth, regulation and differentiation. As a contribution to understanding the structure—function relationship, we report in the present study features of its solution structure and backbone dynamics determined by NMR spectroscopy. Applying multi-dimensional high-resolution NMR techniques on unlabelled and 15N-enriched recombinant human E-FABP, the 1H and 15N resonance assignments were completed. On the basis of 2008 distance restraints, the three-dimensional solution structure of human E-FABP was subsequently obtained (backbone atom root-mean-square deviation of 0.92±0.11Å; where 1Å = 0.1nm), consisting mainly of 10 anti-parallel β-strands that form a β-barrel structure. 15N relaxation experiments (T1, T2 and heteronuclear nuclear Overhauser effects) at 500, 600 and 800MHz provided information on the internal dynamics of the protein backbone. Nearly all non-terminal backbone amide groups showed order parameters S2>0.8, with an average value of 0.88±0.04, suggesting a uniformly low backbone mobility in the nanosecond-to-picosecond time range. Moreover, hydrogen/deuterium exchange experiments indicated a direct correlation between the stability of the hydrogen-bonding network in the β-sheet structure and the conformational exchange in the millisecond-to-microsecond time range. The features of E-FABP backbone dynamics elaborated in the present study differ markedly from those of the phylogenetically closely related heart-type FABP and the more distantly related ileal lipid-binding protein, implying a strong interdependence with the overall protein stability and possibly also with the ligand-binding affinity for members of the lipid-binding protein family.
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June 2002
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Research Article|
June 15 2002
Solution structure and backbone dynamics of human epidermal-type fatty acid-binding protein (E-FABP)
Luis H. GUTIÉRREZ-GONZÁLEZ;
Luis H. GUTIÉRREZ-GONZÁLEZ
∗Institut für Biophysikalische Chemie, Johann Wolfgang Goethe-Universität Frankfurt, Marie-Curie-Strasse 9, D-60439 Frankfurt am Main, Germanyand
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Christian LUDWIG;
Christian LUDWIG
1
∗Institut für Biophysikalische Chemie, Johann Wolfgang Goethe-Universität Frankfurt, Marie-Curie-Strasse 9, D-60439 Frankfurt am Main, Germanyand
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Carsten HOHOFF;
Carsten HOHOFF
2
†Institut für Biochemie, Westfälische Wilhelms-Universität Münster, Wilhelm-Klemm-Strasse 2, D-48149 Münster, Germany
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Martin RADEMACHER;
Martin RADEMACHER
∗Institut für Biophysikalische Chemie, Johann Wolfgang Goethe-Universität Frankfurt, Marie-Curie-Strasse 9, D-60439 Frankfurt am Main, Germanyand
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Thorsten HANHOFF;
Thorsten HANHOFF
†Institut für Biochemie, Westfälische Wilhelms-Universität Münster, Wilhelm-Klemm-Strasse 2, D-48149 Münster, Germany
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Heinz RÜTERJANS;
Heinz RÜTERJANS
∗Institut für Biophysikalische Chemie, Johann Wolfgang Goethe-Universität Frankfurt, Marie-Curie-Strasse 9, D-60439 Frankfurt am Main, Germanyand
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Friedrich SPENER;
Friedrich SPENER
†Institut für Biochemie, Westfälische Wilhelms-Universität Münster, Wilhelm-Klemm-Strasse 2, D-48149 Münster, Germany
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Christian LÜCKE
Christian LÜCKE
3
∗Institut für Biophysikalische Chemie, Johann Wolfgang Goethe-Universität Frankfurt, Marie-Curie-Strasse 9, D-60439 Frankfurt am Main, Germanyand
3To whom correspondence should be addressed (e-mail lueck@bpc.uni-frankfurt.de).
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Publisher: Portland Press Ltd
Received:
January 07 2002
Accepted:
April 02 2002
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London ©2002
2002
Biochem J (2002) 364 (3): 725–737.
Article history
Received:
January 07 2002
Accepted:
April 02 2002
Citation
Luis H. GUTIÉRREZ-GONZÁLEZ, Christian LUDWIG, Carsten HOHOFF, Martin RADEMACHER, Thorsten HANHOFF, Heinz RÜTERJANS, Friedrich SPENER, Christian LÜCKE; Solution structure and backbone dynamics of human epidermal-type fatty acid-binding protein (E-FABP). Biochem J 15 June 2002; 364 (3): 725–737. doi: https://doi.org/10.1042/bj20020039
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