Three-dimensional atomic structure of a catalytic subunit mutant of human protein kinase CK2

Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2133-9. doi: 10.1107/s0907444903018900. Epub 2003 Nov 27.

Abstract

The three-dimensional crystal structure of the triple-point mutant of the catalytic subunit of human protein kinase CK2alpha has been determined at 2.4 A resolution. Microcrystals of mutant CK2 catalytic subunit were obtained by a protein-crystallization method based on thin-film nanotechnology. These microcrystals (of about 20 micro m in diameter) were used for diffraction data collection by means of the microfocus beamline at the ESRF synchrotron. A comparison between the human protein kinase CK2alpha and the corresponding enzyme from a lower organism (Zea mays) is made.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • Casein Kinase II
  • Catalytic Domain
  • Crystallization / methods
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Point Mutation
  • Protein Conformation
  • Protein-Serine-Threonine Kinases / chemistry*
  • Protein-Serine-Threonine Kinases / genetics
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Static Electricity
  • Zea mays / enzymology
  • Zea mays / genetics

Substances

  • Recombinant Proteins
  • Casein Kinase II
  • Protein-Serine-Threonine Kinases