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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of a calcium-deficient form of influenza virus neuraminidase: implications for substrate binding
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Structure of a calcium-deficient form of influenza virus neuraminidase: implications for substrate binding

机译：calcium-deficient结构形式的流感病毒神经氨酸酶:对基质的影响绑定

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摘要

The X-ray structure of influenza virus neuraminidase (NA) isolated from whale, subtype N9, has been determined at 2.2 angstrom resolution and contains a tetrameric protein in the asymmetric unit. In structures of NA determined previously, a calcium ion is observed to coordinate amino acids near the substrate-binding site. In three of the NA monomers determined here this calcium is absent, resulting in structural alterations near the substrate-binding site. These changes affect the conformation of residues that participate in several key interactions between the enzyme and substrate and provide at a molecular level the basis of the structural and functional role of calcium in substrate and inhibitor binding. Several sulfate ions were identified in complex with the protein. These are located in the active site, occupying the space reserved for the substrate (sialic acid) carboxylate, and in positions leading away from the substrate-binding site. These sites offer a new opportunity for the design of inhibitors of influenza virus NA.
机译：流感病毒的x射线结构神经氨酸酶(NA)隔绝鲸鱼,亚型N9,已经确定为2.2埃分辨率和包含一个四聚物的蛋白质不对称单元。决定以前,观察钙离子协调附近的氨基酸substrate-binding网站。单体决定这钙是缺席,导致附近的结构性改变substrate-binding网站。构象参与的残留物几个关键的酶之间的相互作用衬底,并提供在分子水平上的结构和功能作用的基础钙在底物和抑制剂具有约束力。在复杂的几个硫酸盐离子被确定与蛋白质。网站,占领空间的衬底(唾液酸)羧酸盐,在远离substrate-binding领先位置网站。流感病毒抑制剂设计NA。

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