Enzymatic activity with an incomplete catalytic spine: insights from a comparative structural analysis of human CK2α and its paralogous isoform CK2α

• Published in: Molecular and cellular biochemistry Vol. 356; no. 1-2; pp. 57 - 65
• Main Authors: Bischoff, Nils, Raaf, Jennifer, Olsen, Birgitte, Bretner, Maria, Issinger, Olaf-Georg, Niefind, Karsten
• Format: Journal Article
• Language: English
• Published: Boston Springer US 01.10.2011
• Subjects: Adenosine Triphosphate - metabolism; Amino Acid Motifs; Amino Acid Sequence; Binding Sites; Biocatalysis - drug effects; Biochemistry; Biomedical and Life Sciences; Cardiology; Casein Kinase II - antagonists & inhibitors; Casein Kinase II - chemistry; Casein Kinase II - metabolism; Crystallography, X-Ray; Humans; Isoenzymes - antagonists & inhibitors; Isoenzymes - chemistry; Isoenzymes - metabolism; Life Sciences; Ligands; Medical Biochemistry; Models, Molecular; Molecular Sequence Data; Oncology; Phenylalanine - metabolism; Protein Kinase Inhibitors - pharmacology; Sequence Alignment; Structural Homology, Protein; Eukaryotic protein kinases; Catalytic spine; Regulatory spine; Protein kinase CK2; Paralog isoforms of human CK2α; Casein kinase 2

Eukaryotic protein kinases are fundamental factors for cellular regulation and therefore subject of strict control mechanisms. For full activity a kinase molecule must be penetrated by two stacks of hydrophobic residues, the regulatory and the catalytic spine that are normally well conserved among a...