Mutational Analysis of Residues Implicated in the Interaction between Protein Kinase CK2 and Peptide Substrates

Sixteen derivatives of the optimal peptide substrate RRRA-DDSDDDDD in which aspartic acids were singly or multiply substituted by alanine have been assayed for their phosphorylation efficiency by either wild type protein kinase CK2 or CK2 α mutants defective in substrate recognition. With wild type...

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Veröffentlicht in:	Biochemistry (Easton) 1997-09, Vol.36 (39), p.11717-11724
Hauptverfasser:	Sarno, Stefania, Vaglio, Philippe, Marin, Oriano, Issinger, Olaf-Georg, Ruffato, Katia, Pinna, Lorenzo A
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Casein Kinase II Kinetics Models, Molecular Mutagenesis, Site-Directed Peptides - metabolism Protein Binding Protein Conformation Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Structure-Activity Relationship Substrate Specificity
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