Crystal structure of a tetradecameric assembly of the association domain of Ca2+/calmodulin-dependent kinase II
Crystal structure of a tetradecameric assembly of the association domain of Ca2+/calmodulin-dependent kinase II
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DOI：
10.1016/s1097-2765(03)00171-0
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发表时间：
2003-05-01
期刊：
影响因子：
16
通讯作者：
Kuriyan, J
中科院分区：
文献类型：
--
作者：
Hoelz, A;Nairn, AC;Kuriyan, J
本文报道了钙/钙调素依赖性蛋白激酶II（CaMKII）的143个氨基酸残基结合域的晶体结构。结合域形成一个枢纽状的集合体，由两个环组成，每个环有七个原聚体，它们头对头堆叠在一起，并通过广泛的界面保持在一起。通过分析超离心和多角度光散射证实了组装的十四聚体组织。单个原聚体形成楔形结构，连接到激酶结构域的N-末端螺旋片段从楔形结构向组装体的赤道面延伸，这与激酶结构域在第二外环中的排列一致。一个深的和高度保守的口袋内存在的关联结构域可以作为一个对接站点的蛋白质，与CaMKII相互作用。
We report the crystal structure of the 143 residue association domain of Ca2+/calmodulin-dependent protein kinase II (CaMKII). The association domain forms a hub-like assembly, composed of two rings of seven protomers each, which are stacked head to head and held together by extensive interfaces. The tetradecameric organization of the assembly was confirmed by analytical ultracentrifugation and multiangle light scattering. Individual protomers form wedge-shaped structures from which N-terminal helical segments that connect to the kinase domain extend toward the equatorial plane of the assembly, consistent with the arrangement of the kinase domains in a second outer ring. A deep and highly conserved pocket present within the association domain may serve as a docking site for proteins that interact with CaMKII.