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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >Crystal structure of a dimerization domain of human Caprin-1: insights into the assembly of an evolutionarily conserved ribonucleoprotein complex consisting of Caprin-1, FMRP and G3BP1
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Crystal structure of a dimerization domain of human Caprin-1: insights into the assembly of an evolutionarily conserved ribonucleoprotein complex consisting of Caprin-1, FMRP and G3BP1

机译：晶体结构的二聚作用域人类Caprin-1:洞察组装的进化保守的核糖核蛋白组成的复杂Caprin-1、FMRP G3BP1

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摘要

Caprin-1 plays roles in many important biological processes, including cellular proliferation, innate immune response, stress response and synaptic plasticity. Caprin-1 has been implicated in several human diseases, including osteosarcoma, breast cancer, viral infection, hearing loss and neurodegenerative disorders. The functions of Caprin-1 depend on its molecular-interaction network. Direct interactions have been established between Caprin-1 and the fragile X mental retardation protein (FMRP), Ras GAP-activating protein-binding protein 1 (G3BP1) and the Japanese encephalitis virus (JEV) core protein. Here, crystal structures of a fragment (residues 132-251) of Caprin-1, which adopts a novel all-alpha-helical fold and mediates homodimerization through a substantial interface, are reported. Homodimerization creates a large and highly negatively charged concave surface suggestive of a protein-binding groove. The FMRP-interacting sequence motif forms an integral alpha-helix in the dimeric Caprin-1 structure in such a way that the binding of FMRP would not disrupt the homodimerization of Caprin-1. Based on insights from the structures and existing biochemical data, the existence of an evolutionarily conserved ribonucleoprotein (RNP) complex consisting of Caprin-1, FMRP and G3BP1 is proposed. The JEV core protein may bind Caprin-1 at the negatively charged putative protein-binding groove and an adjacent E-rich sequence to hijack the RNP complex.
机译：在许多重要的生物Caprin-1扮演的角色过程,包括细胞增殖、先天免疫反应,应激反应突触可塑性。在一些人类疾病,包括骨肉瘤、乳腺癌、病毒性感染,听力损失和神经退行性疾病。Caprin-1取决于其功能分子间相互作用的网络。之间建立了互动Caprin-1和脆性X智力迟钝Ras GAP-activating蛋白质(FMRP)此种蛋白1 (G3BP1)和乙型脑炎病毒(JEV)核心蛋白质。在这里,晶体结构的一个片段(残留物Caprin-1 132 - 251),采用一种新颖的all-alpha-helical褶皱和协调homodimerization通过大量的接口,报告。和高度带负电荷的凹面此种槽的暗示。FMRP-interacting序列图案形式一个积分在二聚的阿尔法螺旋Caprin-1结构这样FMRP不会的绑定扰乱homodimerization Caprin-1。从结构和现有的见解生化数据的存在进化保守的核糖核蛋白(RNP)组成的复杂Caprin-1、FMRP G3BP1建议。带负电荷的假定的此种槽和一个相邻E-rich序列劫持RNP复杂。

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