Three-dimensional atomic structure of a catalytic subunit mutant of human protein kinase CK2.
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.
Pechkova
Eugenia
E
Fondazione E.L.B.A., Rome, Italy.
Zanotti
Giuseppe
G
Nicolini
Claudio
C
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D047390:Casein Kinase II; D020134:Catalytic Domain; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017354:Point Mutation; D011487:Protein Conformation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D055672:Static Electricity; D003313:Zea mays / Q000201:enzymology / Q000235:genetics
D011994:Recombinant Proteins; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases