Peter Burkhard

Summary

Affiliation: University of Basel
Country: Switzerland

Publications

  1. ncbi request reprint The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges
    P Burkhard
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Basel, CH 4056, Switzerland
    Structure 8:223-30. 2000
  2. ncbi request reprint Improving coiled-coil stability by optimizing ionic interactions
    Peter Burkhard
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH 4056 Basel, Switzerland
    J Mol Biol 318:901-10. 2002
  3. ncbi request reprint Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound
    P Burkhard
    M E Müller Institute for Structural Biology
    J Mol Biol 303:279-86. 2000
  4. ncbi request reprint Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase
    P Burkhard
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH 4056 Basel, Switzerland
    Nat Struct Biol 8:963-7. 2001
  5. ncbi request reprint Coiled coils: a highly versatile protein folding motif
    P Burkhard
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056, Basel, Switzerland
    Trends Cell Biol 11:82-8. 2001
  6. ncbi request reprint Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium
    P Burkhard
    Biozentrum, University of Basel, Klingelbergstrasse 70, Basel, CH 4056, Switzerland
    J Mol Biol 291:941-53. 1999
  7. ncbi request reprint Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium
    P Burkhard
    Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse70, Basel, CH 4056, Switzerland
    J Mol Biol 283:121-33. 1998
  8. ncbi request reprint Removing an interhelical salt bridge abolishes coiled-coil formation in a de novo designed peptide
    Markus Meier
    M E Müller Institute for Structural Biology, University of Basel, Switzerland
    J Struct Biol 137:65-72. 2002
  9. doi request reprint Characterization of the head-to-tail overlap complexes formed by human lamin A, B1 and B2 "half-minilamin" dimers
    Larisa E Kapinos
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, CH 4056 Basel, Switzerland
    J Mol Biol 396:719-31. 2010
  10. ncbi request reprint Structure-based design of peptides that self-assemble into regular polyhedral nanoparticles
    Senthilkumar Raman
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Basel, Switzerland
    Nanomedicine 2:95-102. 2006

Collaborators

Detail Information

Publications28

  1. ncbi request reprint The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges
    P Burkhard
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Basel, CH 4056, Switzerland
    Structure 8:223-30. 2000
    ..The simplicity and regularity of this motif have made it an attractive system to explore some of the fundamental principles of protein folding and stability and to test the principles of de novo design...
  2. ncbi request reprint Improving coiled-coil stability by optimizing ionic interactions
    Peter Burkhard
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH 4056 Basel, Switzerland
    J Mol Biol 318:901-10. 2002
    ..We show that by combining the most favorable inter- and intrahelical salt-bridge arrangements it is possible to design coiled-coil oligomerization domains with improved stability properties...
  3. ncbi request reprint Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound
    P Burkhard
    M E Müller Institute for Structural Biology
    J Mol Biol 303:279-86. 2000
    ..Chloride may be an analog of sulfide, the physiological inhibitor. Finally, these results suggest that OASS represents a new class of PLP-dependent enzymes that is regulated by small anions...
  4. ncbi request reprint Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase
    P Burkhard
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH 4056 Basel, Switzerland
    Nat Struct Biol 8:963-7. 2001
    ..The structures provide the molecular basis for the development of new inhibitors of DDC with better pharmacological characteristics...
  5. ncbi request reprint Coiled coils: a highly versatile protein folding motif
    P Burkhard
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056, Basel, Switzerland
    Trends Cell Biol 11:82-8. 2001
    ..Here we discuss this highly versatile protein folding and oligomerization motif with regard to its structural architecture and how this is related to its biological functions...
  6. ncbi request reprint Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium
    P Burkhard
    Biozentrum, University of Basel, Klingelbergstrasse 70, Basel, CH 4056, Switzerland
    J Mol Biol 291:941-53. 1999
    ....
  7. ncbi request reprint Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium
    P Burkhard
    Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse70, Basel, CH 4056, Switzerland
    J Mol Biol 283:121-33. 1998
    ..The active site cleft of O-acetylserine sulfhydrylase is wider and therefore more exposed to the solvent. A possible binding site for the substrate O-acetylserine is discussed...
  8. ncbi request reprint Removing an interhelical salt bridge abolishes coiled-coil formation in a de novo designed peptide
    Markus Meier
    M E Müller Institute for Structural Biology, University of Basel, Switzerland
    J Struct Biol 137:65-72. 2002
    ..We show that the peptide, while being highly alpha-helical, is no longer able to form a parallel coiled-coil structure but rather assumes an octameric globular helical assembly devoid of any coiled-coil interactions...
  9. doi request reprint Characterization of the head-to-tail overlap complexes formed by human lamin A, B1 and B2 "half-minilamin" dimers
    Larisa E Kapinos
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, CH 4056 Basel, Switzerland
    J Mol Biol 396:719-31. 2010
    ..Furthermore, we suggest that the head-to-tail interaction of the rod end domains represents a principal step in the assembly of cytoplasmic intermediate filament proteins too...
  10. ncbi request reprint Structure-based design of peptides that self-assemble into regular polyhedral nanoparticles
    Senthilkumar Raman
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Basel, Switzerland
    Nanomedicine 2:95-102. 2006
    ..Such peptide nanoparticles are ideally suited for medical applications such as drug targeting and drug delivery systems, such as imaging devices, or they may be used for repetitive antigen display...
  11. doi request reprint Simultaneous formation of right- and left-handed anti-parallel coiled-coil interfaces by a coil2 fragment of human lamin A
    Larisa E Kapinos
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Switzerland
    J Mol Biol 408:135-46. 2011
    ..Such an interface might co-exist with a heterotetrameric left-handed coiled-coil assembly, which is expected to be responsible for the longitudinal A(CN) contact...
  12. pmc Carbohydrate- and conformation-dependent cargo capture for ER-exit
    Christian Appenzeller-Herzog
    Department of Pharmacology and Neurobiology, Biozentrum, University of Basel, CH 4056 Basel, Switzerland
    Mol Biol Cell 16:1258-67. 2005
    ..To our knowledge this is the first documentation of an ER-exit signal in soluble cargo in conjunction with its decoding by a transport receptor...
  13. ncbi request reprint Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation
    Sergei V Strelkov
    Maurice E Müller Institute for Structural Biology, Biozentrum, University of Basel, Switzerland
    J Struct Biol 137:54-64. 2002
    ..In general, the geometrical distortion is confined to about two alpha-helical turns at either side of the stutter. Furthermore, stutters result in a local increase of the coiled-coil radius...
  14. ncbi request reprint Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins
    Sergei V Strelkov
    Maurice E Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH 4056 Basel, Switzerland
    J Mol Biol 343:1067-80. 2004
    ..Based on our data most of these mutations are unlikely to alter the structure of the dimer but may affect essential molecular interactions occurring in later stages of filament assembly and lamina formation...
  15. ncbi request reprint Peptide nanoparticles serve as a powerful platform for the immunogenic display of poorly antigenic actin determinants
    Ulrich Schroeder
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH 4056 Basel, Switzerland
    J Mol Biol 386:1368-81. 2009
    ....
  16. ncbi request reprint X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies
    P Burkhard
    Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, Basel, CH, 4056, Switzerland
    J Mol Biol 295:953-62. 2000
    ..Analysis of the calculated buried surface areas of these related ligands provides an estimated van der Waals contribution to the binding energy of -0.5 kJ/A(2) for non-polar interactions between ligand and protein...
  17. pmc Intersubunit signaling in glutamate-1-semialdehyde-aminomutase
    J Stetefeld
    Department of Structural Biology and M E Müller Institute for Structural Biology, Biozentrum Universität Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland
    Proc Natl Acad Sci U S A 103:13688-93. 2006
    ..Together, they form a molecular switch in which the cofactor acts as a central signal transmitter linking the subunit interface with the gating loop...
  18. pmc Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly
    Sergei V Strelkov
    Maurice E Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH 4056 Basel, Switzerland
    EMBO J 21:1255-66. 2002
    ..These results provide the first insight into the architecture and functioning of IFs at the atomic level...
  19. ncbi request reprint Structural insights into mutations of cystathionine beta-synthase
    Markus Meier
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH 4056, Basel, Switzerland
    Biochim Biophys Acta 1647:206-13. 2003
    ..We have recently solved the crystal structure of a truncated form of this enzyme, which enables us to correlate some of these mutations with the structure...
  20. ncbi request reprint Selective boron-containing thrombin inhibitors--X-ray analysis reveals surprising binding mode
    A von Matt
    Novartis Pharma AG, Basel, Switzerland
    Bioorg Med Chem 8:2291-303. 2000
    ..Nevertheless, these compounds inhibited thrombin in the nM range. The X-ray structure of one of these inhibitors bound to the active side of thrombin reveals that a new binding mode is responsible for these surprising results...
  21. ncbi request reprint Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor
    M Meier
    M E Müller Institute for Structural Biology, University of Basel, Klingelbergstrasse 70 CH 4056 Basel, Switzerland
    J Mol Biol 300:857-65. 2000
    ....
  22. pmc Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein
    M Meier
    M E Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH 4056 Basel, Switzerland
    EMBO J 20:3910-6. 2001
    ..This heme binding motif together with a spatially adjacent oxidoreductase active site motif could explain the regulation of its enzyme activity by redox changes...
  23. ncbi request reprint Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments
    S V Strelkov
    Maurice E Müller Institute for Structural Biology Biozentrum, University of Basel, Klingelbergstrasse 70, Basel, CH 4056, Switzerland
    J Mol Biol 306:773-81. 2001
    ....
  24. ncbi request reprint Towards a molecular description of intermediate filament structure and assembly
    David A D Parry
    Institute of Fundamental Sciences, Massey University, Private Bag 11 222, Palmerston North, New Zealand
    Exp Cell Res 313:2204-16. 2007
    ....
  25. ncbi request reprint Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes
    Arundhati Chattopadhyay
    Institute of Materials Science, University of Connecticut, 97 North Eagleville Road, Storrs, Connecticut 06269 3136, USA
    Biochemistry 46:8315-30. 2007
    ..This finding, in agreement with structural data, suggests for the O-acetylserine sulfhydrylase B-isozyme a higher degree of conformational flexibility linked to catalysis...
  26. ncbi request reprint Sequence comparisons of intermediate filament chains: evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1
    Thomasin A Smith
    Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand
    J Struct Biol 137:128-45. 2002
    ....
  27. pmc Unique stabilizing interactions identified in the two-stranded alpha-helical coiled-coil: crystal structure of a cortexillin I/GCN4 hybrid coiled-coil peptide
    Darin L Lee
    Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada
    Protein Sci 12:1395-405. 2003
    ..7 kcal/mole relative to alanine. These interactions are of critical importance to understanding the stability requirements for coiled-coil folding and in modulating the stability of de novo designed macromolecules containing this motif...
  28. ncbi request reprint Statistical analysis of intrahelical ionic interactions in alpha-helices and coiled coils
    Markus Meier
    The Institute of Materials Science, University of Connecticut, 97 North Eagleville Road, Storrs, CT 06269 3136, USA
    J Struct Biol 155:116-29. 2006
    ..We concluded that the configurations, which have simultaneously a large probability to form the ionic interaction and a frequent occurrence, are those, which have the most stabilising effect. These are the 4RE, 3ER and 4ER interactions...