Huse Morgan, Kuriyan John
Department of Biological Sciences, Stanford University, Palo Alto, California 94305, USA.
Cell. 2002 May 3;109(3):275-82. doi: 10.1016/s0092-8674(02)00741-9.
Protein kinases operate in a large number of distinct signaling pathways, where the tight regulation of their catalytic activity is crucial to the development and maintenance of eukaryotic organisms. The catalytic domains of different kinases adopt strikingly similar structures when they are active. By contrast, crystal structures of inactive kinases have revealed a remarkable plasticity in the kinase domain that allows the adoption of distinct conformations in response to interactions with specific regulatory domains or proteins.
蛋白激酶在大量不同的信号通路中发挥作用，其催化活性的严格调控对于真核生物的发育和维持至关重要。不同激酶的催化结构域在激活时具有惊人相似的结构。相比之下，非活性激酶的晶体结构显示出激酶结构域具有显著的可塑性，这使得它们能够根据与特定调节结构域或蛋白质的相互作用而采用不同的构象。
