Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants.
Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants.
复制标题
N9亚型流感病毒神经氨酸酶和逃逸突变体的精细原子结构。
DOI：
10.1016/0022-2836(91)80069-7
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发表时间：
1991
影响因子：
5.6
通讯作者：
Colman,PM
中科院分区：
文献类型：
--
作者：
Tulip,WR;Varghese,JN;Baker,AT;vanDonkelaar,A;Laver,WG;Webster,RG;Colman,PM
用模拟退火和常规方法对流感病毒N9亚型神经氨酸酶的晶体结构进行了优化，在6.0 ~ 2.2 μ m的分辨率范围内，R因子为0.172。均方根键长与理想值的偏差为0·014 μ m。其结构与N2亚型神经氨酸酶的二级结构元件及其连接方式相似。还报道了用抗神经氨酸酶单克隆抗体选择的几种神经氨酸酶逃逸突变体的三维结构。在每种情况下，与点突变相关的结构变化仅限于突变位点或空间上紧邻突变位点的残基。抗血清在N2和N9亚型之间交叉反应的失败可能与700 μ 2或更大区域的保守连续表面结构的缺失有关。
The crystal structure of the N9 subtype neuraminidase of influenza virus was refined by simulated annealing and conventional techniques to anR-factor of 0·172 for data in the resolution range 6·0 to 2·2 Å. The r.m.s. deviation from ideal values of bond lengths is 0·014 Å. The structure is similar to that of N2 subtype neuraminidase both in secondary structure elements and in their connections. The three-dimensional structures of several escape mutants of neuraminidase, selected with antineuraminidase monoclonal antibodies, are also reported. In every case, structural changes associated with the point mutation are confined to the mutation site or to residues that are spatially immediately adjacent to it. The failure of antisera to cross-react between N2 and N9 subtypes may be correlated with the absence of conserved, contiguous surface structures of area 700 Å2or more.