Recent advances in the characterization of fatty acid-binding proteins (FABPs) by NMR have enabled various research groups to investigate the function of these proteins in aqueous solution. The binding of fatty acid molecules to FABPs, which proceeds through a portal region on the protein surface, is of particular interest. In the present study we have determined the three-dimensional solution structure of human heart-type FABP by multi-dimensional heteronuclear NMR spectroscopy. Subsequently, in combination with data collected on a F57S mutant we have been able to show that different fatty acids induce distinct conformational states of the protein backbone in this portal region, depending on the chain length of the fatty acid ligand. This indicates that during the binding process the protein accommodates the ligand molecule by a ‘selected-fit’ mechanism. In fact, this behaviour appears to be especially pronounced in the heart-type FABP, possibly due to a more rigid backbone structure compared with other FABPs, as suggested by recent NMR relaxation studies. Thus differences in the dynamic behaviours of these proteins may be the key to understanding the variations in ligand affinity and specificity within the FABP family.
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March 2001
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Research Article|
February 22 2001
Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP)
Christian LÜCKE;
Christian LÜCKE
*Institut für Biophysikalische Chemie, Johann Wolfgang Goethe-Universität, Marie-Curie-Strasse 9, 60439 Frankfurt am Main, Germany
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Martin RADEMACHER;
Martin RADEMACHER
*Institut für Biophysikalische Chemie, Johann Wolfgang Goethe-Universität, Marie-Curie-Strasse 9, 60439 Frankfurt am Main, Germany
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Aukje W. ZIMMERMAN;
Aukje W. ZIMMERMAN
†Department of Biochemistry, University of Nijmegen, Geert Groteplein 30, 6525 GA Nijmegen, The Netherlands
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Herman T. B. VAN MOERKERK;
Herman T. B. VAN MOERKERK
†Department of Biochemistry, University of Nijmegen, Geert Groteplein 30, 6525 GA Nijmegen, The Netherlands
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Jacques H. VEERKAMP;
Jacques H. VEERKAMP
†Department of Biochemistry, University of Nijmegen, Geert Groteplein 30, 6525 GA Nijmegen, The Netherlands
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Heinz RÜTERJANS
Heinz RÜTERJANS
1
*Institut für Biophysikalische Chemie, Johann Wolfgang Goethe-Universität, Marie-Curie-Strasse 9, 60439 Frankfurt am Main, Germany
1To whom correspondence should be addressed (e-mail hruet@bpc.uni-frankfurt.de).
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Publisher: Portland Press Ltd
Received:
September 11 2000
Revision Received:
November 06 2000
Accepted:
December 13 2000
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 2001
2001
Biochem J (2001) 354 (2): 259–266.
Article history
Received:
September 11 2000
Revision Received:
November 06 2000
Accepted:
December 13 2000
Citation
Christian LÜCKE, Martin RADEMACHER, Aukje W. ZIMMERMAN, Herman T. B. VAN MOERKERK, Jacques H. VEERKAMP, Heinz RÜTERJANS; Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP). Biochem J 1 March 2001; 354 (2): 259–266. doi: https://doi.org/10.1042/bj3540259
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