Pellicena Patricia, Kuriyan John
Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
Curr Opin Struct Biol. 2006 Dec;16(6):702-9. doi: 10.1016/j.sbi.2006.10.007. Epub 2006 Oct 31.
Protein-protein interactions involving the catalytic domain of protein kinases are likely to be generally important in the regulation of signal transduction pathways, but are rather sparsely represented in crystal structures. Recently determined structures of the kinase domains of the mitogen-activated protein kinase Fus3, the RNA-dependent kinase PKR, the epidermal growth factor receptor and Ca(2+)/calmodulin-dependent protein kinase II have revealed unexpected and distinct mechanisms by which interactions with the catalytic domain can modulate kinase activity.
涉及蛋白激酶催化结构域的蛋白质-蛋白质相互作用在信号转导途径的调控中可能普遍具有重要意义，但在晶体结构中的呈现却相当稀少。最近确定的促分裂原活化蛋白激酶Fus3、RNA依赖性激酶PKR、表皮生长因子受体以及钙/钙调蛋白依赖性蛋白激酶II的激酶结构域结构，揭示了与催化结构域相互作用可调节激酶活性的意外且独特的机制。
