Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate

Journal of Molecular Biology

Volumn 347, Issue 2, 2005, Pages 399-414

  Yde, Christina W ^a   Ermakova, Inessa ^b   Issinger, Olaf Georg ^a   Niefind, Karsten ^b  

^a UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

^b UNIVERSITY OF COLOGNE   (Germany)

Author keywords

Casein kinase 2; Dual cosubstrate specificity; Protein design; Protein kinase CK2; X ray crystallography

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; AMINO ACID DERIVATIVE; CASEIN KINASE II; CYCLIC AMP DEPENDENT PROTEIN KINASE; GUANOSINE TRIPHOSPHATE; ISOLEUCINE; LEUCINE; LIGAND; METHIONINE; MUTANT PROTEIN; PURINE; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; COMPARATIVE STUDY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HUMAN; MAIZE; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

EID: 14644402341     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.003     Document Type: Article

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