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  • 1
    Electronic Resource
    Electronic Resource
    Gene-target recognition among members of the Myc superfamily and implications for oncogenesis (2000)
    [s.l.] : Nature America Inc.
    Nature genetics 24 (2000), S. 113-119 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Myc and Mad family proteins regulate multiple biological processes through their capacity to influence gene expression directly. Here we show that the basic regions of Myc and Mad proteins are not functionally equivalent in oncogenesis, have separable E-box–binding activities and engage ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/72761
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  • 2
    Electronic Resource
    Electronic Resource
    Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis (2000)
    [s.l.] : Nature America Inc.
    Nature structural biology 7 (2000), S. 663-668 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Isocitrate lyase (ICL) plays a pivotal role in the persistence of Mycobacterium tuberculosis in mice by sustaining intracellular infection in inflammatory macrophages. The enzyme allows net carbon gain by diverting acetyl-CoA from β-oxidation of fatty acids into the glyoxylate shunt pathway. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/77964
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  • 3
    Electronic Resource
    Electronic Resource
    Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines (2000)
    [s.l.] : Nature America Inc.
    Nature structural biology 7 (2000), S. 141-146 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The antigen 85 (ag85) complex, composed of three proteins (ag85A, B and C), is a major protein component of the Mycobacterium tuberculosis cell wall. Each protein possesses a mycolyltransferase activity required for the biogenesis of trehalose dimycolate (cord factor), a dominant structure ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/72413
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  • 4
    Electronic Resource
    Electronic Resource
    Crystal structure of a plant catechol oxidase containing a dicopper center (1998)
    [s.l.] : Nature America Inc.
    Nature structural biology 5 (1998), S. 1084-1090 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Catechol oxidases are ubiquitous plant enzymes containing a dinuclear copper center. In the wound-response mechanism of the plant they catalyze the oxidation of a broad range of ortho-diphenols to the corresponding o-quinones coupled with the reduction of oxygen to water. The crystal structures of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/4193
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  • 5
    Electronic Resource
    Electronic Resource
    Rational design of potent human transthyretin amyloid disease inhibitors (2000)
    [s.l.] : Nature America Inc.
    Nature structural biology 7 (2000), S. 312-321 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The human amyloid disorders, familial amyloid polyneuropathy, familial amyloid cardiomyopathy and senile systemic amyloidosis, are caused by insoluble transthyretin (TTR) fibrils, which deposit in the peripheral nerves and heart tissue. Several nonsteroidal anti-inflammatory drugs and structurally ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/74082
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  • 6
    Electronic Resource
    Electronic Resource
    A comparative study of the backbone dynamics of two closely related lipid binding proteins: Bovine heart fatty acid binding protein and porcine ileal lipid binding protein (1999)
    Springer
    Molecular and cellular biochemistry 192 (1999), S. 109-121 
    Details
    ISSN: 1573-4919
    Keywords: lipid binding protein ; 15N relaxation ; protein backbone dynamics ; model-free approach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The backbone dynamics of bovine heart fatty acid binding protein (H-FABP) and porcine ileal lipid binding protein (ILBP) were studied by 15N NMR relaxation (T1 and T2) and steady state heteronuclear 15N{1H} NOE measurements. The microdynamic parameters characterizing the backbone mobility were determined using the ‘model-free’ approach. For H-FABP, the non-terminal backbone amide groups display a rather compact protein structure of low flexibility. In contrast, for ILBP an increased number of backbone amide groups display unusually high internal mobility. Furthermore, the data indicate a higher degree of conformational exchange processes in the μsec-msec time range for ILBP compared to H-FABP. These results suggest significant differences in the conformational stability for these two structurally highly homologous members of the fatty acid binding protein family.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006834708786
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  • 7
    Electronic Resource
    Electronic Resource
    High resolution X-ray studies of mammalian intestinal and muscle fatty acid-binding proteins provide an opportunity for defining the chemical nature of fatty acid: protein interactions (1993)
    Springer
    Molecular and cellular biochemistry 123 (1993), S. 3-13 
    Details
    ISSN: 1573-4919
    Keywords: fatty acid-protein interactions ; X-ray crystallography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The structure ofE. coli-derived rat intestinal fatty acid-binding protein has recently been refined to 1.2 Å without bound fatty acid and to 2.0 Å and 1.75 Å with bound hexadecanoate (palmitate) and 9Z-octadecenoate (oleate), respectively. The structure ofE. coli-derived human muscle fatty acid-binding protein has also been solved to 2.1 Å with a C16 bacterial fatty acid. Both proteins contain 10 anti-parallel β-strands in a+1, +1, +1... motif. The strands are arranged in two β-pleated sheets that are orthogonally oriented. In each case, the fatty acid is enclosed by the β-sheets and is bound to the proteins by feeble forces. These feeble forces consist of (i) a hydrogen bonding network between the fatty acid's carboxylate group, ordered solvent, and side chains of polar/ionizable amino acid residues; (ii) van der Waals contacts between the methylene chain of the fatty acid and the side chain atoms of hydrophobic and aromatic residues; (iii) van der Waals interactions between the ϖ methyl and the component methenyls of the phenyl side chain of a Phe which serves as an adjustable terminal sensor situated over a surface opening or portal connecting interior and exterior solvent; and (iv) van der Waals contacts between methylenes of the alkyl chain and oxygens of ordered waters that have been located inside the binding cavity. These waters are positioned over one face of the ligand and are held in place by hydrogen bonding with one another and with the side chains of protein's polar and ionizable residues. Binding of the fatty acid ligand is associated with minimal adjustments of the positions of main chain or side chain atoms. However, acquisition of ligand is associated with removal of ordered interior solvent suggesting that the free energy of dehydration of the binding site may be as important for the energy of the binding reaction as the free energy of stabilization of the fatty acid: protein complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01076469
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  • 8
    Electronic Resource
    Electronic Resource
    Expression of rat intestinal fatty acid binding protein in E. coli and its subsequent structural analysis: a model system for studying the molecular details of fatty acid-protein interaction (1990)
    Springer
    Molecular and cellular biochemistry 98 (1990), S. 81-93 
    Details
    ISSN: 1573-4919
    Keywords: fatty acid binding protein ; prokaryotic expression vectors ; x-ray crystallography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract A prokaryotic expression vector containing the rec A promoter and a translational enhancer element from the gene 10 leader of bacteriophage T7 was used to direct efficient synthesis of rat intestinal fatty acid binding protein (I-FABP) in E. coli. Expression of I-FABP in E. coli has no apparent, deleterious effects on the organism. High levels of expression of I-FABP mRNA in supE+ strains of E. coli, such as JM101, is associated with suppression of termination at its UGA stop codon. This can be eliminated by using a sup-Estrain as MG1655 and by site-directed mutagenesis of the cDNA to create an in frame UAA stop codon. E. coli-derived rat I-FABP lacks its initiator Met residues. It has been crystallized with and without bound palmitate. High resolution x-ray crystallographic studies of the 131 residue apo- and holo-proteins have revealed the following. I-FABP contains 10 anti-parallel β-strands organized into two orthogonally situated β-sheets. The overall conformation of the protein resembles that of a clam — hence the term β-clam. The bound ligand is located in the interior of the protein. Its carboxylate group forms part of a unique five member hydrogen bonding network consisting of two ordered solvent molecules as well as the side chains of Arg106 and Gln115. The hydrocarbon chain of the bound C16:0 fatty acid has a distinctive bent conformation with a slight left-handed helical twist. This conformation is maintained by interactions with the side chains of a number of hydrophobic and aromatic amino acids. Apo-I-FABP has a similar overall conformation to holo-I-FABP indicating that the β-clam structure is stable even without bound ligand. The space occupied by bound ligand in the core of the holo-protein is occupied by additional ordered solvent molecules in the apo-protein. Differences in the side chain orientations pf several residues located over a potential opening to the cores of the apo- and holo-proteins suggest that solvent may play an important role in the binding mechanism. Comparison of the Cα coordinates of apo- and holo-I-FABP with those of other proteins indicates it is a member of a superfamily that currently includes (i) 10 mammalian intracellular lipid binding proteins, (ii) the photoactive yellow protein from the purple photoautotrophic bacterium Ectothiorhodospira halophila and (iii) a group of extracellular lipid binding proteins from a diverse number of phyla that have a common β ‘barrel’ consisting of 8 anti-parallel β-strands stacked in two nearly orthogonal sheets. In summary, E. coli-derived I-FABP not only represents a useful model for assessing the atomic details of fatty acid-protein interactions and the mechanisms which regulate acquisition and release of this type of ligand, but also structure/function relationships in other superfamily members.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00231371
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  • 9
    Electronic Resource
    Electronic Resource
    13C NMR studies of fatty acid-protein interactions: comparison of homologous fatty acid-binding proteins produced in the intestinal epithelium (1990)
    Springer
    Molecular and cellular biochemistry 98 (1990), S. 101-110 
    Details
    ISSN: 1573-4919
    Keywords: NMR spectroscopy ; fatty acids ; binding proteins ; intestinal absorption
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary A high-resolution, solution-state NMR method for characterizing and comparing the interactions between carboxyl 13C-enriched fatty acids (FA) and individual binding sites on proteins has been developed. The utility of this method results from the high degree of resolution of carboxyl from other carbon resonances and the high sensitivity of FA carboxyl chemical shifts to intermolecular environmental factors such as degree of hydrogen-bonding or hydration, degree of ionization (pH), and proximity to positively-charged or aromatic side-chain moieties in proteins. Information can be obtained regarding binding heterogeneity (structural as well as thermodynamic), binding stoichiometries, relative binding affinities, the ionization behavior of bound FA and protein side-chain moieties, the physical and ionization states of unbound FA, and the exchange rates of FA between protein binding sites and between protein and non-protein acceptors of FA, such as model membranes. Cytosolic fatty acid binding proteins represent an excellent model system for studying and comparing fatty acid-protein interactions. Prokaryotic expression vectors have been used to direct efficient synthesis of several mammalian intestinal FABPs in E. coli. This has enabled us to isolate gram-quantities of purified FABPs, to introduce NMR-observable isotopes, and to generate FABP mutants. The intestine is the only tissue known to contain abundant quantities of more than one FABP homologue in a single cell type. It is likely that these homologous FABPs serve distinct functional roles in intestinal lipid transport. This paper presents comparative 13C NMR results for FA interactions with FABP homologues from intestine, and the functional implications of these analyses are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00231373
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  • 10
    Electronic Resource
    Electronic Resource
    Solution structure of human intestinal fatty acid binding protein: Implications for ligand entry and exit (1997)
    Springer
    Journal of biomolecular NMR 9 (1997), S. 213-228 
    Details
    ISSN: 1573-5001
    Keywords: Human intestinal fatty acid binding protein ; Isotope enrichment ; Multidimensional NMR spectroscopy; ; Sequential assignments ; Solution structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The human intestinal fatty acid binding protein (I-FABP) is a small (131 amino acids) proteinwhich binds dietary long-chain fatty acids in the cytosol of enterocytes. Recently, an alanineto threonine substitution at position 54 in I-FABP has been identified which affects fatty acidbinding and transport, and is associated with the development of insulin resistance in severalpopulations including Mexican-Americans and Pima Indians. To investigate the molecularbasis of the binding properties of I-FABP, the 3D solution structure of the more commonform of human I-FABP (Ala54) was studied by multidimensional NMR spectroscopy.Recombinant I-FABP was expressed from E. coli in the presence and absence of 15N-enriched media. The sequential assignments for non-delipidated I-FABP were completed byusing 2D homonuclear spectra (COSY, TOCSY and NOESY) and 3D heteronuclear spectra(NOESY-HMQC and TOCSY-HMQC). The tertiary structure of human I-FABP wascalculated by using the distance geometry program DIANA based on 2519 distance constraintsobtained from the NMR data. Subsequent energy minimization was carried out by using theprogram SYBYL in the presence of distance constraints. The conformation of human I-FABPconsists of 10 antiparallel β-strands which form two nearly orthogonal β-sheets offive strands each, and two short α-helices that connect the β-strands A and B. Theinterior of the protein consists of a water-filled cavity between the two β-sheets. TheNMR solution structure of human I-FABP is similar to the crystal structure of rat I-FABP.The NMR results show significant conformational variability of certain backbone segmentsaround the postulated portal region for the entry and exit of fatty acid ligand.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018666522787
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