首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8
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Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8

机译:猪轮状病毒CRW-8菌株唾液酸结合域(VP8 *)的结晶和初步X射线衍射分析

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摘要

Rotavirus recognition and attachment to host cells involves interaction with the spike protein VP4 that projects outwards from the surface of the virus particle. An integral component of these spikes is the VP8* domain, which is implicated in the direct recognition and binding of sialic acid-containing cell-surface carbohydrates and facilitates subsequent invasion by the virus. The expression, purification, crystallization and preliminary X-ray diffraction analysis of VP8* from porcine CRW-8 rotavirus is reported. Diffraction data have been collected to 2.3 Å resolution, enabling the determination of the VP8* structure by molecular replacement.
机译:轮状病毒的识别和对宿主细胞的附着涉及与从病毒颗粒表面向外突出的刺突蛋白VP4的相互作用。这些尖峰的组成部分是VP8 *域,与含唾液酸的细胞表面碳水化合物的直接识别和结合有关,并有助于病毒随后的入侵。报道了猪CRW-8轮状病毒VP8 *的表达,纯化,结晶和初步X射线衍射分析。收集到的衍射数据达到2.3Å分辨率,可通过分子置换确定VP8 *结构。

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