Crystallization and low-resolution structure of an effector-caspase/P35 complex: similarities and differences to an initiator-caspase/P35 complex.

Eddins MJ; Lemongello D; Friesen PDFisher AJ

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Crystallization and low-resolution structure of an effector-caspase/P35 complex: similarities and differences to an initiator-caspase/P35 complex.

机译：结晶和低分辨率的结构的和effector-caspase / P35区域复杂:相似之处一个initiator-caspase / P35区域复杂的差异。

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The aspartate-specific caspases play a pivotal role in the execution of programmed cell death and therefore constitute important targets for the control of apoptosis. Upon ectopic expression, baculovirus P35 inhibits apoptosis in phylogenetically diverse organisms by suppressing the proteolytic activity of the cellular caspases in a cleavage-dependent mechanism. After cleavage by caspase, the P35 fragments remain bound to the target caspase, forming an inhibitory complex that sequesters the caspase from further activity. Crystals of a complex between P35 and Sf-caspase-1, an insect effector-caspase, were grown. A 5.2 A resolution structure of this inhibitory complex was determined by molecular-replacement methods. The structure reveals few regions of interaction between the two proteins, much like that observed in the structure of the recently solved human initiator-caspase/P35 complex. In the effector-caspase/P35 complex structure presented here, the P35 molecule shifts towards a loop that is conserved in effector caspases but absent in initiator caspase. This shift could strengthen interactions between the two proteins and may explain the preference of P35 for inhibiting effector-caspases.

机译：还存在aspartate-specific发挥关键在程序性细胞死亡的执行因此构成的重要目标细胞凋亡的控制。表情,杆状病毒P35区域抑制细胞凋亡系统不同的生物体通过抑制的蛋白水解活性细胞还存在在一个cleavage-dependent机制。半胱天冬酶,P35区域保持绑定到碎片半胱天冬酶目标,形成一个抑制复杂由此进一步的半胱天冬酶活动。昆虫effector-caspase Sf-caspase-1,增长。抑制复杂的决定了molecular-replacement方法。揭示了几个地区之间的交互两种蛋白质,类似观察最近解决了人类的结构initiator-caspase / P35区域复杂。effector-caspase / P35区域复杂的结构在这里,P35区域分子转向一个循环是守恒的效应还存在,但没有在吗引发剂半胱天冬酶。两个蛋白质之间的相互作用和可能为抑制解释P35区域的偏好effector-caspases。

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《Acta crystallographica.Section D. Biological crystallography》 |2002年第2期|299-302|共4页
作者
Eddins MJ; Lemongello D; Friesen PDFisher AJ;
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作者单位

Department of Chemistry, University of California, Davis, CA 95616, USA.;

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正文语种英语
中图分类化学;
关键词
Caspase 1; Initiator Caspases; CaspasesCASP1 geneCDK-Activating Kinase Assembly Factor MAT1Viral ProteinsEffector CaspasesCrystallization;

机译：半胱天冬酶1;还存在引发剂;CaspasesCASP1geneCDK-Activating激酶装配因素MAT1Viral ProteinsEffectorCaspasesCrystallization;

Crystallization and low-resolution structure of an effector-caspase/P35 complex: similarities and differences to an initiator-caspase/P35 complex.

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