动态激活细胞凋亡：cIAP1 的构象集合与弹簧加载机制相关联。
Dynamic activation of apoptosis: conformational ensembles of cIAP1 are linked to a spring-loaded mechanism.
机构信息
Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, USA.
出版信息
Nat Struct Mol Biol. 2014 Dec;21(12):1022-3. doi: 10.1038/nsmb.2925.
Abstract
cIAP1 undergoes a dramatic conformational change during activation that is now shown to be due to the dynamic and metastable nature of the closed form of the enzyme. The discovery of such a striking mechanism for functional control was enabled by state-of-the-art enzymological and biophysical methods.
摘要
cIAP1 在激活过程中经历了剧烈的构象变化，现在证明这种变化是由于酶的封闭形式的动态和亚稳态性质所致。这种用于功能控制的惊人机制的发现得益于最先进的酶学和生物物理方法。
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本文引用的文献
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Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine.变构调节 E2:E3 相互作用促进了连续泛素化机器。
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Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination.拮抗剂诱导 cIAP1 构象变化，促进自身泛素化。
Science. 2011 Oct 21;334(6054):376-80. doi: 10.1126/science.1207862.
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Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment.cIAP2 环指结构域的结构揭示了与泛素结合酶（E2）募集相关的构象变化。
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IAP antagonists target cIAP1 to induce TNFalpha-dependent apoptosis.IAP拮抗剂靶向cIAP1以诱导肿瘤坏死因子α依赖性凋亡。
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