H Nar

Summary

Affiliation: Boehringer Ingelheim

Publications

  1. ncbi request reprint Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor
    H Nar
    Department of Medicinal Chemistry, Boehringer Ingelheim Pharma KG, Biberach, Germany
    J Mol Biol 312:743-51. 2001
  2. ncbi request reprint Structural basis for inhibition promiscuity of dual specific thrombin and factor Xa blood coagulation inhibitors
    H Nar
    Department of Medicinal Chemistry, Boehringer Ingelheim Pharma KG, 88397 Biberach an der Riss, Germany
    Structure 9:29-37. 2001
  3. ncbi request reprint Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation
    H Nar
    Department of Chemistry, Boehringer Ingelheim Pharma KG, Biberach, Germany
    J Mol Biol 297:683-95. 2000
  4. ncbi request reprint Crystal structure of bisphosphorylated IGF-1 receptor kinase: insight into domain movements upon kinase activation
    A Pautsch
    Boehringer Ingelheim Pharma KG Deutschland, Birkendorferstrasse 65, D 88400 Biberach, Germany
    Structure 9:955-65. 2001
  5. pmc Zinc plays a key role in human and bacterial GTP cyclohydrolase I
    G 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
  6. ncbi request reprint Crystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthase
    T Ploom
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, Martinsried, 82152, Germany
    J Mol Biol 286:851-60. 1999
  7. ncbi request reprint The metal site of Pseudomonas aeruginosa azurin, revealed by a crystal structure determination of the Co(II) derivative and Co-EPR spectroscopy
    N Bonander
    Department of Biochemistry, Goteborg University, Sweden
    Proteins 27:385-94. 1997
  8. ncbi request reprint Structure and mechanism of GTP cyclohydrolase I of Escherichia coli
    H Nar
    Max Planck Institut fur Biochemie, Martinsried, Federal Republic of Germany
    Biochem Soc Trans 24:37S. 1996
  9. pmc Active site topology and reaction mechanism of GTP cyclohydrolase I
    H Nar
    Max Planck Institut fur Biochemie, Martinsried, Federal Republic of Germany
    Proc Natl Acad Sci U S A 92:12120-5. 1995
  10. pmc Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis
    H Nar
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Martinsried Germany
    EMBO J 13:1255-62. 1994

Collaborators

  • A Gils
  • W Wienen
  • S Weinkauf
  • A Messerschmidt
  • A Pautsch
  • Soohee Lee
  • T Ploom
  • G Auerbach
  • A Bacher
  • M Fischer
  • N Bonander
  • R Huber
  • C Hammann
  • J F Rippmann
  • G W Canters
  • B G Karlsson
  • W Meining
  • C Schmid
  • A Schnapp
  • T Oppliger
  • S Hobbie
  • C Daiber
  • W J Rettig
  • J Birk
  • P Garin-Chesa
  • B Guilliard
  • M Bauer
  • A Romero
  • L Bachmann
  • L C Tsai
  • L Sjölin
  • V Langer
  • G van Pouderoyen
  • F X Gomis Rüth
  • T Den Blaauwen
  • J Sanders-Loehr
  • G Gilardi
  • D Bürgisser
  • B Thony
  • C W Heizmann
  • N Blau
  • F S Mathews
  • M van de Kamp
  • A P Kalverda
  • R Durley
  • S Eberhardt
  • W Gimbel
  • H Ritz
  • H W Lahm
  • T Werner
  • A Lommen
  • C W Hilbers
  • S S Wijmenga

Detail Information

Publications25

  1. ncbi request reprint Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor
    H 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...
  2. ncbi request reprint Structural basis for inhibition promiscuity of dual specific thrombin and factor Xa blood coagulation inhibitors
    H 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...
  3. ncbi request reprint Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation
    H Nar
    Department of Chemistry, Boehringer Ingelheim Pharma KG, Biberach, Germany
    J Mol Biol 297:683-95. 2000
    ....
  4. ncbi request reprint Crystal structure of bisphosphorylated IGF-1 receptor kinase: insight into domain movements upon kinase activation
    A 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...
  5. pmc Zinc plays a key role in human and bacterial GTP cyclohydrolase I
    G 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...
  6. ncbi request reprint Crystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthase
    T 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...
  7. ncbi request reprint The metal site of Pseudomonas aeruginosa azurin, revealed by a crystal structure determination of the Co(II) derivative and Co-EPR spectroscopy
    N 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...
  8. ncbi request reprint Structure and mechanism of GTP cyclohydrolase I of Escherichia coli
    H Nar
    Max Planck Institut fur Biochemie, Martinsried, Federal Republic of Germany
    Biochem Soc Trans 24:37S. 1996
  9. pmc Active site topology and reaction mechanism of GTP cyclohydrolase I
    H 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...
  10. pmc Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis
    H 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...
  11. ncbi request reprint Crystal structure analysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus
    A 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...
  12. ncbi request reprint Atomic structure of GTP cyclohydrolase I
    H 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...
  13. ncbi request reprint X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa
    H 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...
  14. ncbi request reprint Elucidation of crystal packing by X-ray diffraction and freeze-etching electron microscopy. Studies on GTP cyclohydrolase I of Escherichia coli
    W 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...
  15. ncbi request reprint Studies on GTP cyclohydrolase I of Escherichia coli
    C Schmid
    Technische Universitat Munchen, Lehrstuhl fur Organische Chemie und Biochemie, Garching, Federal Republic of Germany
    Adv Exp Med Biol 338:157-62. 1993
  16. ncbi request reprint Characterization and crystal structure of zinc azurin, a by-product of heterologous expression in Escherichia coli of Pseudomonas aeruginosa copper azurin
    H 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...
  17. ncbi request reprint Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 A resolution
    H 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...
  18. ncbi request reprint Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis
    J 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...
  19. ncbi request reprint 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 flip
    H 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...
  20. ncbi request reprint The pathway from GTP to tetrahydrobiopterin: three-dimensional structures of GTP cyclohydrolase I and 6-pyruvoyl tetrahydropterin synthase
    G 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...
  21. ncbi request reprint X-ray structure determination and characterization of the Pseudomonas aeruginosa azurin mutant Met121Glu
    B 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...
  22. ncbi request reprint Structural and functional consequences of mutations in 6-pyruvoyltetrahydropterin synthase causing hyperphenylalaninemia in humans. Phosphorylation is a requirement for in vivo activity
    T 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...
  23. ncbi request reprint Crystal structures of modified apo-His117Gly and apo-His46Gly mutants of Pseudomonas aeruginosa azurin
    C 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...
  24. ncbi request reprint X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosa
    C Hammann
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Martinsried bei Munchen, Germany
    J Mol Biol 255:362-6. 1996
    ....
  25. ncbi request reprint Complete sequential 1H and 15N nuclear magnetic resonance assignments and solution secondary structure of the blue copper protein azurin from Pseudomonas aeruginosa
    M 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...