Related ArticlesThree-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy.
Eur J Biochem. 1995 May 15;230(1):266-80
Authors: Lassen D, Lücke C, Kveder M, Mesgarzadeh A, Schmidt JM, Specht B, Lezius A, Spener F, Rüterjans H
The three-dimensional structure of the holo form of recombinant cellular bovine heart fatty-acid-binding protein (H-FABPc), a polypeptide of 133 amino acid residues with a molecular mass of 15 kDa, has been determined by multidimensional homonuclear and heteronuclear NMR spectroscopy applied to uniformly 15N-labeled and unlabeled protein. A nearly complete set of 1H and 15N chemical shift assignments was obtained. A total of 2329 intramolecular distance constraints and 42 side-chain chi 1 dihedral-angle constraints were derived from cross-relaxation and J coupling information. 3D nuclear Overhauser enhancement and exchange spectroscopy combined with heteronuclear multiple-quantum coherence (NOESY-HMQC) experiments, performed on a sample of uniformly 13C-labeled palmitic acid bound to unlabeled cellular heart fatty-acid-binding protein revealed 10 intermolecular contacts that determine the orientation of the bound fatty acid. An ensemble of protein conformations was calculated with the distance-geometry algorithm for NMR applications (DIANA) using the redundant dihedral-angle constraint (REDAC) strategy. After docking the fatty acid into the protein, the protein-ligand arrangement was subject to distance-restrained energy minimization. The overall conformation of the protein is a beta-barrel consisting of 10 antiparallel beta-strands which form two nearly orthogonal beta-sheets of five strands each. Two short helices form a helix-turn-helix motif in the N-terminal region of the polypeptide chain. The palmitic acid is bound within the protein in a U-shaped conformation close to the two helices. The obtained solution structure of the protein is consistent with a number of fatty-acid-binding-protein crystal structures.
[NMR paper] NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: evi
NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: evidence for conformational heterogeneity in the native state.
Related Articles NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: evidence for conformational heterogeneity in the native state.
Biochemistry. 2005 Feb 22;44(7):2369-77
Authors: Li H, Frieden C
(19)F-Nuclear magnetic resonance (NMR) studies have been carried out after incorporation of 4-(19)F-phenylalanine into the intestinal fatty acid binding protein (IFABP), a...
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[NMR paper] NMR assignment and structural characterization of the fatty acid binding protein from
NMR assignment and structural characterization of the fatty acid binding protein from the flight muscle of Locusta migratoria.
Related Articles NMR assignment and structural characterization of the fatty acid binding protein from the flight muscle of Locusta migratoria.
J Biomol NMR. 2003 Apr;25(4):355-6
Authors: Lücke C, Kizilbash N, van Moerkerk HT, Veerkamp JH, Hamilton JA
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[NMR paper] Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C
Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C NMR and fluorescence study.
Related Articles Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C NMR and fluorescence study.
Biochemistry. 2001 Oct 23;40(42):12604-11
Authors: Beringhelli T, Goldoni L, Capaldi S, Bossi A, Perduca M, Monaco HL
Two different groups of liver fatty acid-binding proteins (L-FABPs) are known: the mammalian type and the basic type. Very few members of this second group of L-FABPs have been...
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[NMR paper] Bound water in apo and holo bovine heart fatty-acid-binding protein determined by het
Bound water in apo and holo bovine heart fatty-acid-binding protein determined by heteronuclear NMR spectroscopy.
Related Articles Bound water in apo and holo bovine heart fatty-acid-binding protein determined by heteronuclear NMR spectroscopy.
Eur J Biochem. 1998 Feb 1;251(3):781-6
Authors: Mesgarzadeh A, Pfeiffer S, Engelke J, Lassen D, Rüterjans H
Two- and three-dimensional heteronuclear NMR experiments have been performed to identify internally bound water molecules in the solution structure of bovine heart fatty-acid-binding protein...
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[NMR paper] Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein
Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
Biochemistry. 1997 Feb 25;36(8):2278-90
Authors: Hodsdon ME, Cistola DP
The backbone dynamics of the liganded (holo) and unliganded (apo) forms of Escherichia...
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[NMR paper] Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein
Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
Biochemistry. 1997 Feb 25;36(8):2278-90
Authors: Hodsdon ME, Cistola DP
The backbone dynamics of the liganded (holo) and unliganded (apo) forms of Escherichia...
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[NMR paper] The NMR solution structure of intestinal fatty acid-binding protein complexed with pa
The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: application of a novel distance geometry algorithm.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: application of a novel distance geometry algorithm.
J Mol Biol. 1996 Dec 6;264(3):585-602
Authors: Hodsdon ME, Ponder JW, Cistola DP
The three-dimensional solution structure of rat...
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[NMR paper] The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver:
The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy.
Related Articles The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy.
J Biomol NMR. 1993 May;3(3):271-84
Authors: Andersen KV, Poulsen FM
The 3D structure of bovine recombinant acyl-coenzyme A binding protein has been determined using multidimensional heteronuclear magnetic...
Three-dimensional structure of bovine heart fatty-acid-binding protein with bound pal
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