Light scattering and transmission electron microscopy studies reveal a mechanism for calcium/calmodulin‐dependent protein kinase II self‐association

Calmodulin (CaM)‐kinase II holoenzymes composed of either α or β subunits were analyzed using light scattering to determine a mechanism for self‐association. Under identical reaction conditions, only αCaM‐kinase II holoenzymes self‐associated. Self‐association was detected at a remarkably low enzyme...

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Veröffentlicht in:	Journal of neurochemistry 2001-03, Vol.76 (5), p.1364-1375
Hauptverfasser:	Hudmon, Andy, Kim, Sally A., Kolb, Stephen J., Stoops, James K., Waxham, M. Neal
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence autoinhibition autophosphorylation Binding Sites Biological and medical sciences calcium Calcium - metabolism Calcium-Calmodulin-Dependent Protein Kinase Type 2 Calcium-Calmodulin-Dependent Protein Kinases - chemistry Calcium-Calmodulin-Dependent Protein Kinases - metabolism Calcium-Calmodulin-Dependent Protein Kinases - ultrastructure Calmodulin - metabolism calmodulin‐dependent protein kinase II Catalytic Domain Cell physiology Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration ischemia Kinetics Light Microscopy, Electron Models, Molecular Molecular and cellular biology Peptides - chemistry Peptides - metabolism Protein Binding Protein Conformation Scattering, Radiation self‐association Signal transduction translocation
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