A A Antson

Summary

Affiliation: University of York
Country: UK

Publications

  1. ncbi Circular assemblies
    A A Antson
    Department of Chemistry, University of York, UK
    Curr Opin Struct Biol 6:142-50. 1996
  2. ncbi Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA
    A A Antson
    York Structural Biology Laboratory, Department of Chemistry, University of York, UK
    Nature 401:235-42. 1999
  3. ncbi Single-stranded-RNA binding proteins
    A A Antson
    York Structural Biology Laboratory, Department of Chemistry, University of York, York, YO10 5DD, UK
    Curr Opin Struct Biol 10:87-94. 2000
  4. ncbi The structure of trp RNA-binding attenuation protein
    A A Antson
    Department of Chemistry, University of York, UK
    Nature 374:693-700. 1995
  5. ncbi Structure of the human S100A12-copper complex: implications for host-parasite defence
    O V Moroz
    Department of Chemistry, University of York, York YO10 5YW, England
    Acta Crystallogr D Biol Crystallogr 59:859-67. 2003
  6. ncbi The three-dimensional structure of human S100A12
    O V Moroz
    Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, England
    Acta Crystallogr D Biol Crystallogr 57:20-9. 2001
  7. ncbi The structure of S100A12 in a hexameric form and its proposed role in receptor signalling
    O V Moroz
    Department of Chemistry, University of York, York YO10 5DD, England
    Acta Crystallogr D Biol Crystallogr 58:407-13. 2002
  8. ncbi 11-fold symmetry of the trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis determined by X-ray analysis
    A A Antson
    Department of Chemistry, University of York, U K
    J Mol Biol 244:1-5. 1994
  9. ncbi Understanding the mechanism of ice binding by type III antifreeze proteins
    A A Antson
    Structural Biology Laboratory Department of Chemistry, University of York, Heslington, York Y01 5DD, UK
    J Mol Biol 305:875-89. 2001
  10. ncbi Crystallization and preliminary X-ray diffraction analysis of human calcium-binding protein S100A12
    O V Moroz
    Structural Biology Centre, Department of Chemistry, University of York, York YO1 5DD, England
    Acta Crystallogr D Biol Crystallogr 56:189-91. 2000

Collaborators

Detail Information

Publications11

  1. ncbi Circular assemblies
    A A Antson
    Department of Chemistry, University of York, UK
    Curr Opin Struct Biol 6:142-50. 1996
    ..In most cases the circular organization generates a new biophysical property and a specific biological function which have presumably been selected by evolution...
  2. ncbi Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA
    A A Antson
    York Structural Biology Laboratory, Department of Chemistry, University of York, UK
    Nature 401:235-42. 1999
    ....
  3. ncbi Single-stranded-RNA binding proteins
    A A Antson
    York Structural Biology Laboratory, Department of Chemistry, University of York, York, YO10 5DD, UK
    Curr Opin Struct Biol 10:87-94. 2000
    ..These structures revealed wonderfully satisfying patterns of the ability of proteins to accommodate RNA bases, with the sugar-phosphate backbone often adopting conformations that are different from the classical double helix...
  4. ncbi The structure of trp RNA-binding attenuation protein
    A A Antson
    Department of Chemistry, University of York, UK
    Nature 374:693-700. 1995
    ..It is argued that upon binding, the messenger RNA target forms a matching circle in which eleven U/GAG repeats are bound to the surface of the protein ondecamer modified by the binding of L-tryptophan...
  5. ncbi Structure of the human S100A12-copper complex: implications for host-parasite defence
    O V Moroz
    Department of Chemistry, University of York, York YO10 5YW, England
    Acta Crystallogr D Biol Crystallogr 59:859-67. 2003
    ..The results suggest that copper binding may be essential for the functional role of S100A12 and probably the other calgranulins in the early immune response...
  6. ncbi The three-dimensional structure of human S100A12
    O V Moroz
    Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, England
    Acta Crystallogr D Biol Crystallogr 57:20-9. 2001
    ..The precise role of S100A12 in cell behaviour is yet undefined, as is the case for the whole family, although it has been shown that the interaction of S100A12 with the RAGE receptor is implicated in inflammatory response...
  7. ncbi The structure of S100A12 in a hexameric form and its proposed role in receptor signalling
    O V Moroz
    Department of Chemistry, University of York, York YO10 5DD, England
    Acta Crystallogr D Biol Crystallogr 58:407-13. 2002
    ..It is proposed that the S100A12 hexameric assembly might interact with three extracellular domains of the receptor, bringing them together into large trimeric assemblies...
  8. ncbi 11-fold symmetry of the trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis determined by X-ray analysis
    A A Antson
    Department of Chemistry, University of York, U K
    J Mol Biol 244:1-5. 1994
    ..The consequence is that the TRAP molecule has 11-fold symmetry and contains 11 subunits...
  9. ncbi Understanding the mechanism of ice binding by type III antifreeze proteins
    A A Antson
    Structural Biology Laboratory Department of Chemistry, University of York, Heslington, York Y01 5DD, UK
    J Mol Biol 305:875-89. 2001
    ..Our modelling studies, performed with the refined structure, confirm that type III AFP can make energetically favourable interactions with several ice surfaces...
  10. ncbi Crystallization and preliminary X-ray diffraction analysis of human calcium-binding protein S100A12
    O V Moroz
    Structural Biology Centre, Department of Chemistry, University of York, York YO1 5DD, England
    Acta Crystallogr D Biol Crystallogr 56:189-91. 2000
    ..6 c = 64.2 A. There are two monomers per asymmetric unit, with a solvent content of 57.9%. The crystals diffract to at least 2.2 A resolution and complete X-ray data have been collected to 2.5 A on a conventional laboratory source...
  11. ncbi Regulatory features of the trp operon and the crystal structure of the trp RNA-binding attenuation protein from Bacillus stearothermophilus
    X P Chen
    Department of Biological Sciences, State University of New York, Buffalo, NY, 14260, USA
    J Mol Biol 289:1003-16. 1999
    ..As expected, the TRAP:RNA complex from B. stearothermophilus is significantly more thermostable than that from B. subtilis, with optimal binding occurring at 70 degrees C...