Research Topics
Species | H NarSummaryAffiliation: Boehringer Ingelheim Publications
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Detail Information
Publications
Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitorH Nar
Department of Medicinal Chemistry, Boehringer Ingelheim Pharma KG, Biberach, Germany
J Mol Biol 312:743-51. 2001..The present structure enables us to aid the design of potent and selective inhibitors for MMP-12...- Structural basis for inhibition promiscuity of dual specific thrombin and factor Xa blood coagulation inhibitorsH Nar
Department of Medicinal Chemistry, Boehringer Ingelheim Pharma KG, 88397 Biberach an der Riss, Germany
Structure 9:29-37. 2001..Simultaneous direct inhibition of thrombin and factor Xa by synthetic proteinase inhibitors as a novel approach to antithrombotic therapy could result in potent anticoagulants with improved pharmacological properties... - Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivationH Nar
Department of Chemistry, Boehringer Ingelheim Pharma KG, Biberach, Germany
J Mol Biol 297:683-95. 2000.... - Crystal structure of bisphosphorylated IGF-1 receptor kinase: insight into domain movements upon kinase activationA Pautsch
Boehringer Ingelheim Pharma KG Deutschland, Birkendorferstrasse 65, D 88400 Biberach, Germany
Structure 9:955-65. 2001..Structures of the homologous insulin receptor kinase (IRK) exist in an open, unphosphorylated form and a closed, trisphosphorylated form... 
Zinc plays a key role in human and bacterial GTP cyclohydrolase IG Auerbach
Abteilung Strukturforschung, Max Planck Institut fur Biochemie, Am Klopferspitz 18a, D 82152 Martinsried, Germany
Proc Natl Acad Sci U S A 97:13567-72. 2000..It may also be involved in the hydrolytic release of formate from the intermediate, 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate, and in the consecutive Amadori rearrangement of the ribosyl moiety...- Crystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthaseT Ploom
Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, Martinsried, 82152, Germany
J Mol Biol 286:851-60. 1999..Kinetic studies with dihydroneopterin monophosphate reveal that the triphosphate moiety of the substrate is necessary for enzyme specifity... - The metal site of Pseudomonas aeruginosa azurin, revealed by a crystal structure determination of the Co(II) derivative and Co-EPR spectroscopyN Bonander
Department of Biochemistry, Goteborg University, Sweden
Proteins 27:385-94. 1997..23; gy' = 3.83; gz' = 1.995, and hyperfine splittings Ax' = 31; Ay' = 20-30; Az' = 53 G) and indicates that the ligand field is close to axial... - Structure and mechanism of GTP cyclohydrolase I of Escherichia coliH Nar
, Martinsried, Federal Republic of Germany
Biochem Soc Trans 24:37S. 1996 - Active site topology and reaction mechanism of GTP cyclohydrolase IH Nar
Max Planck Institut fur Biochemie, Martinsried, Federal Republic of Germany
Proc Natl Acad Sci U S A 92:12120-5. 1995..The gamma-phosphate of GTP may be involved in the subsequent Amadori rearrangement of the carbohydrate side chain by activating the hydroxyl group of Ser-135... - Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesisH Nar
Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Martinsried Germany
EMBO J 13:1255-62. 1994..Close to the metal, but apparently not liganding it, are residues Cys42, Glu133 (both from A) and His89 (from B), which might serve as proton donors and acceptors during catalysis... - Crystal structure analysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutusA Romero
Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Martinsried bei Munchen, Germany
J Mol Biol 236:1196-211. 1994..One of the copper ligands, His96, is exposed to the surface and lies in the centre of a cluster of seven hydrophobic residues... - Atomic structure of GTP cyclohydrolase IH Nar
Max Planck Institute für Biochemie, Abteilung Strukturforschung, Martinsried, Germany
Structure 3:459-66. 1995..The initial reaction is catalyzed by GTP cyclohdrolase I (GTP-CH-I) and involves the chemically complex transformation of the purine into the pterin ring system... - X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosaH Nar
Max Planck Institut fur Biochemie, Abteilung Strukturforschung Martinsried b München, Germany
J Mol Biol 218:427-47. 1991..The implications for electron transfer properties of the protein are discussed in terms of the mutation site and the packing of the molecules within the tetramer... - Elucidation of crystal packing by X-ray diffraction and freeze-etching electron microscopy. Studies on GTP cyclohydrolase I of Escherichia coliW Meining
Department of Chemistry Technical University of Munich, Garching, Federal Republic of Germany
J Mol Biol 253:208-18. 1995..The procedure for this analysis as well as possible pitfalls are discussed in detail... - Studies on GTP cyclohydrolase I of Escherichia coliC Schmid
, , Garching, Federal Republic of Germany
Adv Exp Med Biol 338:157-62. 1993 - Characterization and crystal structure of zinc azurin, a by-product of heterologous expression in Escherichia coli of Pseudomonas aeruginosa copper azurinH Nar
Max Planck Institut fur Biochemie, Abteilung für Strukturforschung, Martinsried, Federal Republic of Germany
Eur J Biochem 205:1123-9. 1992..It moves by 0.03 nm towards the zinc, thereby reducing its distance to the metal from 0.29 nm in the copper protein to 0.23 nm in the derivative... - Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 A resolutionH Nar
Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Martinsried bei Munchen, Germany
FEBS Lett 306:119-24. 1992..At low pH, no broadening is observed. This may indicate that here the interconversion is fast on the NMR timescale... - Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosisJ F Rippmann
Department of Oncology Research, Boehringer Ingelheim Pharma KG, Biberach, Germany
Cell Growth Differ 11:409-16. 2000..The results of all of the three lines of investigation show that the catalytic activity of Pin1 is essential for tumor cell survival and entry into mitosis... - Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flipH Nar
Max Planck Institut fur Biochemie, Martinsried bei Munchen, Germany
J Mol Biol 221:765-72. 1991..The structure of the remainder of the azurin molecule, including the copper binding site, is not significantly affected by this transition... - The pathway from GTP to tetrahydrobiopterin: three-dimensional structures of GTP cyclohydrolase I and 6-pyruvoyl tetrahydropterin synthaseG Auerbach
Max Planck Institut fur Biochemie, Martinsried, Germany
Biol Chem 378:185-92. 1997..Here we review the structural and mechanistic information on the biosynthetic pathway from GTP to BH4 on the basis of the recently determined crystal structures of CYH and PTPS... - X-ray structure determination and characterization of the Pseudomonas aeruginosa azurin mutant Met121GluB G Karlsson
Department of Biochemistry and Biophysics, Goteborg University, Sweden
Biochemistry 36:4089-95. 1997..The spectroscopic changes in this pH interval are consistent with a two-state model. From the pH dependence of the optical and EPR spectra, pKa = 5.0 for the glutamic acid in the oxidized protein was determined... - Structural and functional consequences of mutations in 6-pyruvoyltetrahydropterin synthase causing hyperphenylalaninemia in humans. Phosphorylation is a requirement for in vivo activityT Oppliger
Department of Pediatrics, University of Zurich, Switzerland
J Biol Chem 270:29498-506. 1995..Our results demonstrate that PTPS undergoes protein phosphorylation and requires additional, not yet identified post-translational modification(s) for its in vivo function... - Crystal structures of modified apo-His117Gly and apo-His46Gly mutants of Pseudomonas aeruginosa azurinC Hammann
Max Planck Institut fur Biochemie, Abteilung für Struktur Forschung, Martinsried bei Munchen, Germany
J Mol Biol 266:357-66. 1997..This shift causes a slight rearrangement of the monomers within the tetramer such that one local dyad becomes a crystallographic dyad parallel to the c-axis. This leads to a change in the space group from P2(1)2(1)2(1) to P2(1)2(1)2... - X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosaC Hammann
Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Martinsried bei Munchen, Germany
J Mol Biol 255:362-6. 1996.... - Complete sequential 1H and 15N nuclear magnetic resonance assignments and solution secondary structure of the blue copper protein azurin from Pseudomonas aeruginosaM van de Kamp
Department of Chemistry, Gorlaeus Laboratories, Leiden University, The Netherlands
Biochemistry 31:10194-207. 1992..The implications of these observations for the assignment of azurin resonance Raman spectra, the rigidity of the blue copper site, and the electron transfer mechanism of azurin are discussed...