Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1979734 | Current Opinion in Structural Biology | 2006 | 8 Pages |
Abstract
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 Ca2+/calmodulin-dependent protein kinase II have revealed unexpected and distinct mechanisms by which interactions with the catalytic domain can modulate kinase activity.
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Authors
Patricia Pellicena, John Kuriyan,