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首页> 外文期刊>Proteins: Structure, Function, and Genetics >Insights into a highly conserved network of hydrogen bonds in the agonist binding site of nicotinic acetylcholine receptors: a structural and theoretical study.
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Insights into a highly conserved network of hydrogen bonds in the agonist binding site of nicotinic acetylcholine receptors: a structural and theoretical study.

机译：深入了解烟碱乙酰胆碱受体激动剂结合位点中氢键网络的高度保守：结构和理论研究。

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摘要

Structural and theoretical studies on the geometrical features of a hydrogen-bond network occurring in the binding site of nicotinic acetylcholine receptors (nAChRs) and composed of interconnected WxPD (Trp-x-Pro-Asp) and SWyz (Ser-Trp-yz) sequences from loops A and B, respectively, have been carried out. Multiple sequence alignments using as template the sequence of the apoform of Aplysia californica acetylcholine binding protein (Ac-AChBP) show the strict conservation of serine and tryptophan residues of the loop B SWyz sequence. Considering a sample of 19 high resolution AChBP structures, the strong conformational preferences of the key tryptophan residue has been pointing out, whatever the form, free or bounded, of AChBP. The geometry of the motif hydrogen-bond network has been characterized through the analyses of seven distances. The robustness of the various hydrogen-bond interactions is pointed out, the one involving the aspartate carboxylate group and the serine residue being the shortest of the network. The role of a cooperative effect involving a NH(His145)…OH (Ser142) hydrogen bond is highlighted. Density functional theory calculations on several simplified models based on the motif hydrogen-bond network allow probing the importance of the various hydrogen-bond interactions. The removal of the Ser142 hydroxyl group induces strong structural rearrangements, in agreement with the structural observations. Molecular electrostatic potential calculations on model systems highlight the importance of a cooperative effect in the whole hydrogen-bond network. More precisely, the key role of the Ser142 hydroxyl group, involved in several hydrogen bonds, is underlined.
机译：结构和理论研究的氢键网络的几何特征发生在烟碱乙酰胆碱受体（nAChRs）的结合位点，并由相互联系的WxPD（Trp-x-Pro-Asp）和SWyz（Ser-Trp-yz）序列组成分别从循环A和循环B执行。使用加州夜蛾乙酰胆碱结合蛋白（Ac-AChBP）的Apoform序列作为模板进行的多个序列比对表明，严格保守了环B SWyz序列的丝氨酸和色氨酸残基。考虑到19种高分辨率AChBP结构的样品，无论色散形式是AChBP，关键色氨酸残基的强烈构象偏好都被指出。通过七个距离的分析，表征了氢键基序网络的几何形状。指出了各种氢键相互作用的稳健性，其中涉及天冬氨酸羧酸酯基团和丝氨酸残基的是网络中最短的。强调了涉及NH（His145）…OH（Ser142）氢键的协同作用的作用。基于基序氢键网络的几种简化模型的密度泛函理论计算，可以探究各种氢键相互作用的重要性。与结构观察结果一致，Ser142羟基的去除引起强烈的结构重排。在模型系统上的分子静电势计算强调了在整个氢键网络中协同效应的重要性。更确切地说，强调了涉及多个氢键的Ser142羟基的关键作用。

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