Crystal structure of Apaf-1 caspase recruitment domain:: An α-helical Greek key fold for apoptotic signaling
Crystal structure of Apaf-1 caspase recruitment domain:: An α-helical Greek key fold for apoptotic signaling
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DOI：
10.1006/jmbi.1999.3177
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发表时间：
1999-10-29
影响因子：
5.6
通讯作者：
Joshua-Tor, L
中科院分区：
文献类型：
--
作者：
Vaughn, DE;Rodriguez, J;Joshua-Tor, L
Apaf-1的半胱天冬酶募集结构域（CARD）与半胱天冬酶-9的CARD结合以触发导致凋亡性细胞死亡的蛋白水解级联。我们报告的晶体结构的Apaf-1 CARD在1.3埃的分辨率，解决了两个元素的多波长异常色散（MAD）的X射线衍射实验。该CARD采用具有Creek键的六螺旋束折叠，拓扑结构围绕广泛的疏水核心。这种折叠，我们称之为“死亡折叠”，存在于介导凋亡信号传导中相互作用的其他结构域中，尽管序列同一性非常低。从基于结构的比对，我们确定了保守的模式，其特征的死亡折叠及其子类。与Ig折叠一样，它提供了：一个刚性的结构支架，在其上组装了不同的识别表面。(C)北京：科学出版社.
The caspase recruitment domain (CARD) of Apaf-1 binds to the CARD of caspase-9 to trigger a proteolytic cascade that leads to apoptotic cell death. We report the crystal structure of the Apaf-1 CARD at 1.3 Angstrom resolution, solved in a two-element multiwavelength anomalous dispersion (MAD) X-ray diffraction experiment. This CARD adopts a six-helix bundle fold with Creek key, topology surrounding an extensive hydrophobic core. This fold, which we call the "death fold", is found in other domains that mediate interactions in apoptotic signaling despite very low sequence identity. From a structure-based alignment, we identify conserved patterns that characterize the death fold and its subclasses. Like the Ig-fold, it provides:a rigid structural scaffold upon which diverse recognition surfaces are assembled. (C) 1999 Academic Press.