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Solution structure of bovine heart fatty acid-binding protein (H-FABPc)

  • Cellular Fatty Acid-Binding Proteins II
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Abstract

Fatty acid-binding protein (FABP) from bovine heart, a 15 kDa cytoplasmic protein has been investigated by multidimensional homonuclear and heteronuclear NMR-spectroscopy. Perdeuterated palmitic acid has been used as fatty acid ligand. The tertiary structure has been determined from distance geometry calculations with the variable target functions algorithm (DIANA) [1] utilizing 1027 interproton distance constraints, which were obtained from1H-homo-nuclear NOESY spectra. Overlapping NOE crosspeaks were assigned by heteronuclear multidimensional NMR-experiments with a15N-labelled sample. The tertiary structure resembles a β-barrel (β-clam) consisting of ten anti-parallel β-strands and a short helix-turn-helix motif. The β-strands are arranged in two nearly orthogonal β-sheets composed of 5 strands each. The solution structure is compared with the x-ray cyrstal structure of bovine heart [4] and rat intestinal FABPs.

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Abbreviations

DOF-COSY:

Double Quantum Filtered Correlated Spectroscopy

TOCSY:

Total Correlated Spectroscopy

NOE:

Nuclear Overhauser Enhancement

NOESY:

Nuclear Overhauser Enhancement and Exchange Spectroscopy

HMQC:

Heteronuclear Multiple Quantum Coherence

FABP:

Fatty Acid-Binding Protein

FABPc :

Cellular Fatty Acid-Binding Protein

H-FABPc :

Cellular Heart Fatty Acid-Binding Protein

I-FABPc :

Cellular Intestinal Fatty Acid-Binding Protein

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Lassen, D., Lücke, C., Kromminga, A. et al. Solution structure of bovine heart fatty acid-binding protein (H-FABPc). Mol Cell Biochem 123, 15–22 (1993). https://doi.org/10.1007/BF01076470

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