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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DOI: https://doi.org/10.1007/BF01076470