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Solution structure of fatty acid-binding protein from human brain

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Cellular Lipid Binding Proteins

Part of the book series: Developments in Molecular and Cellular Biochemistry ((DMCB,volume 38))

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 of ten antiparallel β-strands (βA to βJ) that form two almost orthogonal β-sheets, a helix-turn-helix motif that closes the β-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. (Mol Cell Biochem 239: 61–68, 2002)

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Abbreviations

2D:

two-dimensional

3D:

three-dimensional

CRBP:

cellular retinol-binding protein

CRABP:

cellular retinoic acid-binding protein

DHA:

docosahexaenoic acid

FA:

fatty acid

FABP:

fatty acid-binding protein

A-FABP:

adipocyte-type FABP

B-FABP:

brain-type FABP

H-FABP:

heart-type FABP

I-FABP:

intestinal-type FABP

ILBP:

ileal lipid-binding protein

L-FABP:

liver-type FABP

M-FABP:

myelin-type FABP

HSQC:

heteronuclear single-quantum correlation

NOE:

nuclear Overhauser effect

NOESY:

nuclear Overhauser enhancement and exchange spectroscopy

TOCSY:

total correlation spectroscopy

RMSD:

root-mean-square deviation

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Author information

Authors and Affiliations

  1. Institut für Biophysikalische Chemie, Johann Wolfgang Goethe-Universität, Frankfurt a. M., Germany

    Martin Rademacher, Heinz Rüterjans & Christian Lücke

  2. Department of Biochemistry, University of Nijmegen, Nijmegen, The Netherlands

    Aukje W. Zimmerman & Jacques H. Veerkamp

  3. Institut für Biophysikalische Chemie, Johann Wolfgang Goethe-Universität, Marie-Curie-Str. 9, 60439, Frankfurt a. M., Germany

    Christian Lücke

Authors
  1. Martin Rademacher
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  2. Aukje W. Zimmerman
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  3. Heinz Rüterjans
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  4. Jacques H. Veerkamp
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  5. Christian Lücke
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Editor information

Editors and Affiliations

  1. Department of Physiology Cardiovascular Research Institute Maastricht (CARIM), Maastricht University, PO. Box 616, 6200 MD, Maastricht, The Netherlands

    Jan F. C. Glatz

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Rademacher, M., Zimmerman, A.W., Rüterjans, H., Veerkamp, J.H., Lücke, C. (2002). Solution structure of fatty acid-binding protein from human brain. In: Glatz, J.F.C. (eds) Cellular Lipid Binding Proteins. Developments in Molecular and Cellular Biochemistry, vol 38. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-9270-3_8

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  • DOI: https://doi.org/10.1007/978-1-4419-9270-3_8

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-4868-9

  • Online ISBN: 978-1-4419-9270-3

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