Generation of mutants of CK2α which are dependent on the β-subunit for catalytic activity

Molecular and Cellular Biochemistry

Volumn 227, Issue 1-2, 2001, Pages 13-19

  Sarno, S ^a   Ghisellini, P ^b   Cesaro, L ^a   Battistutta, R ^a   Pinna, L ^a  

^a UNIVERSITY OF PADOVA   (Italy)

^b UNIVERSITY OF GENOA   (Italy)

Author keywords

catalytic subunit; Casein kinase 2; CK2 mutants; N terminal domain; Protein kinase CK2

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; CASEIN KINASE II; HOLOENZYME; PROTEIN KINASE; PEPTIDE; PROTEIN SERINE THREONINE KINASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA CHAIN; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SUBUNIT; GEL FILTRATION; HUMAN; MAIZE; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MUTANT; TRANSPORT KINETICS; AMINO ACID SEQUENCE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GEL CHROMATOGRAPHY; GENE DELETION; GENETICS; KINETICS; MOLECULAR GENETICS; MUTATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CONFORMATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

ZEA MAYS;

ALANINE; AMINO ACID SEQUENCE; CASEIN KINASE II; CATALYTIC DOMAIN; CHROMATOGRAPHY, GEL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GENE DELETION; HUMANS; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; ZEA MAYS;

EID: 0035543859     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1013136117395     Document Type: Article

References (11)

1. Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
2. Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution
3. Mechanism of CDK activation revealed by the structure of a cyclin A-CDK2 complex
4. Biochemical evidence that the N-terminal segments of the α subunit and the β subunit play interchangeable roles in the activation of protein kinase CK2
5. Protein kinase CK2 mutants defective in substrate recognition. Purification and kinetic analysis
6. Assay of protein kinases and phosphatases using specific peptide substrates
7. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
8. The crystal structure of the complex of Zea mays alpha subunit with a fragment of human beta subunit provides the clue to the architecture of protein kinase CK2 holoenzyme
9. GTP plus water mimic ATP in the active site of protein kinase CK2
10. Raster3D - Photorealistic molecular graphics
11. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures