Crystallization of Sendai virus HN protein complexed with monoclonal antibody Fab fragments.
Crystallization of Sendai virus HN protein complexed with monoclonal antibody Fab fragments.
复制标题
仙台病毒 HN 蛋白与单克隆抗体 Fab 片段复合的结晶。
DOI：
10.1016/0042-6822(89)90541-2
复制
发表时间：
1989
期刊：
影响因子：
3.7
通讯作者：
Portner,A
中科院分区：
文献类型：
--
作者：
Laver,WG;Thompson,SD;Murti,KG;Portner,A
仙台病毒的血凝素-神经氨酸酶（HN）蛋白在通过蛋白水解消化疏水氨基末端锚序列（S. D. Thompson，W. G. Laver，K. G. Murti，A. Portner，J.Virol.62，4653-4660，1988）。可溶性HN以二聚体和四聚体的形式存在，并且用这些形式中的每一种进行的结晶试验迄今为止产生无定形材料。与单克隆抗体的Fab片段复合的二聚体形成长针状晶体。到目前为止，这些都不适合于X射线衍射分析，但结果表明，HN分子从副粘病毒，即使不结晶，可能，当与Fab片段复合，在某些情况下，产生晶体适合于X射线衍射分析。
The hemagglutinin-neuraminidase (HN) protein of Sendai virus has been isolated from virus particles in a biologically active soluble form after removal by proteolytic digestion of the hydrophobic amino-terminal anchor sequence (S. D. Thompson, W. G. Laver, K. G. Murti, A. Portner,J. Virol.62, 4653–4660, 1988). The soluble HN exists as both dimers and tetramers, and crystallization trials with each of these forms have so far yielded amorphous material. Dimers complexed with Fabfragments of a monoclonal antibody formed long needle crystals. So far, these are not suitable for X-ray diffraction analysis but the results suggest that HN molecules from paramyxoviruses, even if not crystallizable, may, when complexed with Fabfragments, in some cases yield crystals suitable for X-ray diffraction analysis.