Structure of the heterodimeric complex between CAD domains of CAD and ICAD
Structure of the heterodimeric complex between CAD domains of CAD and ICAD
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DOI：
10.1038/77957
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发表时间：
2000-08-01
期刊：
影响因子：
--
通讯作者：
Yamazaki, T
中科院分区：
文献类型：
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作者：
Otomo, T;Sakahira, H;Yamazaki, T
我们在这里提出的CAD结构域的半胱天冬酶激活的脱氧核糖核酸酶（CAD）和CAD结构域的抑制剂（ICAD）之间的复合物的结构，由核磁共振光谱测定。这两个结构域采用非常相似的折叠，其由α-螺旋和β-折叠组成，并且在复合物中并排排列。值得注意的是，在复合物中，CAD β-折叠一端的β 2链上的正电荷和ICAD β-折叠相对端周围的负电荷配对。在CAD或ICAD上，在该界面处的带电氨基酸的点突变阻止了功能性CAD-ICAD复合物的形成。这意味着CAD和ICAD的CAD域之间的相互作用是在复杂的CAD正确折叠的重要步骤。
We present here the structure of the complex between the CAD domain of caspase activated deoxyribonuclease (CAD) and the CAD domain of its inhibitor (ICAD), determined by nuclear magnetic resonance spectroscopy. The two domains adopt a very similar fold, which consists of an alpha-helix and a beta-sheet, and are aligned side by side in the complex. Notably the positive charges on the strand beta 2 at one end of the beta-sheet of CAD and negative charges around the opposite end of the beta-sheet of ICAD are paired in the complex. Point mutations of the charged amino acids at this interface, on either CAD or ICAD, prevented formation of the functional CAD-ICAD complex. This implies that the interaction between the CAD domains of CAD and ICAD is an essential step in the correct folding of CAD in the complex.