Catalytic Independent Functions of a Protein Kinase as Revealed by a Kinase-dead Mutant: Study of the Lys72His Mutant of cAMP-dependent Kinase

A highly conserved lysine in subdomain II is required for high catalytic activity among the protein kinases. This lysine interacts directly with ATP and mutation of this residue leads to a classical “kinase-dead” mutant. This study describes the biophysical and functional properties of a kinase-dead...

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Veröffentlicht in:	Journal of molecular biology 2005-09, Vol.351 (5), p.1110-1122
Hauptverfasser:	Iyer, Ganesh H., Garrod, Siv, Woods, Virgil L., Taylor, Susan S.
Format:	Artikel
Sprache:	eng
Schlagworte:	3-Phosphoinositide-Dependent Protein Kinases Adenosine Triphosphate - chemistry Amino Acid Sequence Binding Sites cAMP-dependent protein kinase Catalysis Catalytic Domain catalytic mechanism Circular Dichroism Cyclic AMP - metabolism Cyclic AMP-Dependent Protein Kinases - chemistry Electrophoresis, Polyacrylamide Gel Escherichia coli - enzymology Escherichia coli - genetics Histidine - chemistry Hydrogen - chemistry hydrogen–deuterium exchange Kinetics Ligands Lysine - chemistry Mass Spectrometry Models, Molecular Molecular Sequence Data Mutation Peptides - chemistry Phosphorylation Protein Binding protein dynamics Protein Structure, Tertiary Protein-Serine-Threonine Kinases - chemistry Spectrometry, Fluorescence Surface Plasmon Resonance Time Factors
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