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首页> 外文期刊>Biochemistry >Positions 94-98 of the Lactose Repressor N-Subdomain Monomer-Monomer Interface Are Critical for Allosteric Communications
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Positions 94-98 of the Lactose Repressor N-Subdomain Monomer-Monomer Interface Are Critical for Allosteric Communications

机译：乳糖阻遏物N-亚域单体-单体界面的位置94-98对于变构通讯至关重要

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摘要

The central region of the Lad N-subdomain monomer-monomer interface includes residues К84, V94, V95, V96, S97, and М98. The side chains of these residues line the β-strands at this interface and interact to create a network of hydrophobic, charged, and polar interactions that significantly rearranges in different functional states of Lad. Prior work showed that converting К84 to an apolar residue or converting V96 to an acidic residue impedes the allosteric response to inducer. Thus, we postulated that a disproportionate number of substitutions in this region of the monomer-monomer interface would alter the complex features of the Lac! allosteric response. To explore this hypothesis, acidic, basic, polar, and apolar mutations were introduced at positions 94-98. Despite their varied locations along the
机译：Lad N-亚结构域单体-单体界面的中心区域包括残基К84，V94，V95，V96，S97和М98。这些残基的侧链在该界面处排列β链，并相互作用以形成疏水，带电和极性相互作用的网络，该网络在Lad的不同功能状态下会发生明显的重排。先前的工作表明，将К84转化为非极性残基或将V96转化为酸性残基阻碍了对诱导物的变构反应。因此，我们推测在单体-单体界面的该区域中不成比例的取代数目将改变Lac！的复杂特征。变构反应。为了探索这一假设，在位置94-98引入了酸性，碱性，极性和非极性突变。尽管沿途位置各异

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