Kjell Håkansson

Summary

Affiliation: University of Copenhagen
Country: Denmark

Publications

  1. ncbi request reprint The strand-helix motif is a recurring theme in biological hydrolysis. Does the conformation of the Ramachandran outlier enhance its electrophilicity?
    Kjell Håkansson
    August Krogh Institute, LCMF, Universitetsparken 13, DK 210 0, Oe, Copenhagen, Denmark
    Int J Biol Macromol 30:273-7. 2002
  2. ncbi request reprint Homology modeling of Na,K-ATPase: a putative third sodium binding site suggests a relay mechanism compatible with the electrogenic profile of Na+ translocation
    K O Håkansson
    Biomembrane Center, August Krogh Institute, University of Copenhagen, Denmark
    Ann N Y Acad Sci 986:163-7. 2003
  3. ncbi request reprint The crystallographic structure of Na,K-ATPase N-domain at 2.6A resolution
    Kjell O Hakansson
    August Krogh Institute, Copenhagen University, Universitetsparken 13, DK 2100 OE, Copenhagen, Denmark
    J Mol Biol 332:1175-82. 2003
  4. ncbi request reprint The three-dimensional structure of catalase from Enterococcus faecalis
    Kjell O Hakansson
    August Krogh Institute, Copenhagen University, Universitetsparken 13, DK 2100 Kbh O, Denmark
    Acta Crystallogr D Biol Crystallogr 60:1374-80. 2004
  5. pmc Crystallization of mutant forms of glutaredoxin Grx1p from yeast
    Kjell O Hakansson
    Institute of Molecular Biology, August Krogh Building, University of Copenhagen, Universitetsparken 13, DK 2100 Copenhagen O, Denmark
    Acta Crystallogr Sect F Struct Biol Cryst Commun 62:920-2. 2006
  6. ncbi request reprint Structure of glutaredoxin Grx1p C30S mutant from yeast
    Kjell O Hakansson
    Department of Molecular Biology, August Krogh Building, University of Copenhagen, Universitetsparken 13, DK 2100 Copenhagen Ø, Denmark
    Acta Crystallogr D Biol Crystallogr 63:288-94. 2007

Detail Information

Publications6

  1. ncbi request reprint The strand-helix motif is a recurring theme in biological hydrolysis. Does the conformation of the Ramachandran outlier enhance its electrophilicity?
    Kjell Håkansson
    August Krogh Institute, LCMF, Universitetsparken 13, DK 210 0, Oe, Copenhagen, Denmark
    Int J Biol Macromol 30:273-7. 2002
    ..According to this, the Ramachandran values reflect the orientation of one of the backbone amino group that stabilises the oxyanion intermediate of catalysis...
  2. ncbi request reprint Homology modeling of Na,K-ATPase: a putative third sodium binding site suggests a relay mechanism compatible with the electrogenic profile of Na+ translocation
    K O Håkansson
    Biomembrane Center, August Krogh Institute, University of Copenhagen, Denmark
    Ann N Y Acad Sci 986:163-7. 2003
    ..This relay mechanism may therefore be compatible with the electrogenic profile of Na(+) translocation...
  3. ncbi request reprint The crystallographic structure of Na,K-ATPase N-domain at 2.6A resolution
    Kjell O Hakansson
    August Krogh Institute, Copenhagen University, Universitetsparken 13, DK 2100 OE, Copenhagen, Denmark
    J Mol Biol 332:1175-82. 2003
    ..The positions of key residues are discussed in relation to the pattern of hydrophobicity, charge and sequence conservation of the molecular surface. The structure of a hexahistidine tag binding to nickel ions is presented...
  4. ncbi request reprint The three-dimensional structure of catalase from Enterococcus faecalis
    Kjell O Hakansson
    August Krogh Institute, Copenhagen University, Universitetsparken 13, DK 2100 Kbh O, Denmark
    Acta Crystallogr D Biol Crystallogr 60:1374-80. 2004
    ..mirabilis. The solvent structure in the active site is identical in the four subunits but differs from that found in other catalases. The structural consequences of the Ramachandran outlier Ser196 are discussed...
  5. pmc Crystallization of mutant forms of glutaredoxin Grx1p from yeast
    Kjell O Hakansson
    Institute of Molecular Biology, August Krogh Building, University of Copenhagen, Universitetsparken 13, DK 2100 Copenhagen O, Denmark
    Acta Crystallogr Sect F Struct Biol Cryst Commun 62:920-2. 2006
    ..0 A (synchrotron radiation) and 2.7 A (rotating-anode generator), respectively. In contrast, rxYFP-Grx1p formed crystals at high pH in MgSO(4) which diffract synchrotron radiation to 2.7 A...
  6. ncbi request reprint Structure of glutaredoxin Grx1p C30S mutant from yeast
    Kjell O Hakansson
    Department of Molecular Biology, August Krogh Building, University of Copenhagen, Universitetsparken 13, DK 2100 Copenhagen Ø, Denmark
    Acta Crystallogr D Biol Crystallogr 63:288-94. 2007
    ..Conserved residues are clustered on one side of the active site...