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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Protein L mutants for the crystallization of antibody fragments.
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Protein L mutants for the crystallization of antibody fragments.

机译:蛋白突变体的结晶抗体片段。

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In many cases, antibody and their complexes can be crystallized and their structure determined without major difficulties. The remaining problematic cases may be approached through techniques such as of combinatorial complex crystallization which uses immunoglobulin binding proteins (IBP). The range of lattices that can be made using this method can be expanded by engineering mutants of IBP domains. We have designed Peptostreptococcus magnus protein L (PpL) mutants with altered immunoglobulin light chain binding characteristics. While the wild type PpL has two binding sites, some of the mutants contact the light chain via only one site. Other mutants have combinations of weakened first and second binding sites that modify their crystallization properties and their packing mode. In this study, we have selected PpL mutants with different behavior and that are most useful for crystallization and we present the various packing modes obtained so far.
机译:在许多情况下,抗体及其复合物结晶和结构决定的没有重大的困难。有问题的情况下可能会接近等技术组合的复杂结晶,使用免疫球蛋白绑定蛋白质(IBP)。用这种方法可以扩展工程突变体IBP域。设计蛋白质消化链球菌属magnus L(PpL)突变体免疫球蛋白水平改变了光链绑定的特征。PpL类型有两个结合位点,一些通过只有一个突变体与轻链联系网站。第一次和第二次绑定修改他们的网站结晶性能和包装模式。不同的行为和最有用的结晶和我们不同包装模式到目前为止获得的。

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