Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II.

摘要: Ca2+/calmodulin activated protein kinase II (CaMKII) is an oligomeric with a unique holoenyzme architecture. The subunits of CaMKII are bound together into the holoenzyme by association domain, C-terminal region approximately 140 residues in polypeptide. Single particle analyses electron micrographs have suggested previously that forms dodecamer contains two stacked 6-fold symmetric rings. In contrast, recent crystal structure isolated domain mouse CaMKIIalpha has revealed tetradecameric assembly 7-fold this study, we determined Caenorhabditis elegans and it too tetradecamer. We also show microscopy its fully assembled form but without domains, either from expression bacteria or following their removal proteolysis, domains speculate held state interactions N-terminal 1-335 allows to convert more stable form.