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Lattice‐translocation defects in specific crystals of the catalytic head domain of influenza neuraminidase
Acta Crystallographica Section D ( IF 2.2 ) Pub Date : 2020-11-02 , DOI: 10.1107/s2059798320011869
Linghui Li 1 , Shuliu Dai 2 , George F Gao 1 , Jiawei Wang 2
Affiliation  

Neuraminidase (NA) inhibitors are one of the two major classes of antivirals available for the treatment and prevention of influenza. X‐ray crystal structure determination of NA head domains and their complexes with various inhibitors are of importance for the design and optimization of anti‐influenza drugs. However, the globular tetrameric properties of NA head domains may produce crystals with pathological imperfections, lattice‐translocation defects, making structure determination no longer straightforward. In this report, using a crystal of the NA head domain from the Wuhan Asiatic toad influenza virus as an example, the identification and solution of this type of crystal pathology are presented. Furthermore, its underlying mechanism of formation is explored.

中文翻译:

流感神经氨酸酶催化头部结构域特定晶体的晶格移位缺陷

神经氨酸酶(NA)抑制剂是可用于治疗和预防流感的两大类抗病毒药之一。X射线晶体结构的NA头域及其与各种抑制剂的配合物的确定对于抗流感药物的设计和优化至关重要。但是,NA头域的球形四聚体性质可能会产生具有病理缺陷,晶格易位缺陷的晶体,从而使结构确定不再简单。在本报告中,以武汉亚洲蟾蜍流感病毒的NA头域晶体为例,介绍了这种晶体病理学的鉴定和解决方案。此外,探讨了其潜在的形成机理。
更新日期:2020-11-02
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