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首页> 外文期刊>Biochemistry >Exploring the Role of Glutamine 50 in the Homeodomain-DNA Interface: Crystal Structure of Engrailed (Gln50->Ala) Complex at 2.0A
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Exploring the Role of Glutamine 50 in the Homeodomain-DNA Interface: Crystal Structure of Engrailed (Gln50->Ala) Complex at 2.0A

机译：探索谷氨酰胺50在同源域-DNA接口中的作用：在2.0A的晶体（GLN50-> ALA）复合物的晶体结构

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摘要

We have determined the crystal structure of a complex containing the engrailed homodomain Gln50->Ala variant (QA50) bound to the wild-type optimal DNA site (TAATTA) at 2.0 A resolution. Biochemical and genetic studies by other groups have suggested that residue 50 is an important determinant of differential DNA-binding specificity among homeodomains (distinguishing among various sites of the general from TAATNN). However, biochemical studies of the QA50 variant had revealed that it binds almost as tightly as the wild-type protein and with only modest changes in specificity. We have now determined the crystal structure of the QA50 vairant to help understand the role of residue 50 in site-specific recognition. Our cocrystal structure shows some interesting changes in the water structure at the site of substitution and shows some changes in the conformations of neighboring side chains. However, the structure, like the QA50 biochemical data, suggests that Gln50 plays a relatively modest role in determining the affinity and specificity of the engrailed homeodomain.
机译：我们已经确定了含有诱导的同性恋GLN50-> ALA变体（QA50）的复合物的晶体结构，在2.0分辨率下与野生型最佳DNA位点（Taatta）结合。其他群体的生化和遗传研究表明残留物50是双透析液之间的差异DNA结合特异性的重要决定因素（区分从陶氏的一般地点）。然而，QA50变体的生化研究表明，它几乎紧密地作为野生型蛋白质结合，并且只有适度的特异性变化。我们现在确定了QA50竞争者的晶体结构，以帮助了解残留物50在特定现场识别中的作用。我们的Cocrystal结构表明了替代部位的水结构有趣的变化，并显示了相邻侧链的构象的一些变化。然而，与QA50生物化学数据一样，该结构表明GLN50在确定诱惑的同性恋的亲和力和特异性方面发挥着相对谦虚的作用。

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