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首页> 外文期刊>Biochemistry >Cation-π Interactions in Lipocalins: Structural and Functional Implications
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Cation-π Interactions in Lipocalins: Structural and Functional Implications

机译：脂蛋白的阳离子-π相互作用：结构和功能的含义。

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摘要

The cation-π interaction impacts protein folding, structural stability, specificity, and molecular recognition. Cation-π interactions have been overlooked in the lipocalin family. To fill this gap, these interactions were analyzed in the 113 crystal and solution structures from the lipocalin family. The cation-π interactions link previously identified structurally conserved regions and reveal new motifs, which are beyond the reach of a sequence alignment algorithm. Functional and structural significance of the interactions were tested experimentally in human tear lipocalin (TL). TL, a prominent and promiscuous lipocalin, has a key role in lipid binding at the ocular surface. Ligand binding modulation through the loop AB at the "open" end of the barrel has been erroneously attributed solely to electrostatic interactions. Data revealed that the interloop cation-π interaction in the pair Phe28-Lys108 contributes significantly to stabilize the holo-conformation of the loop AB. Numerous energetically significant and conserved cation-n interactions were uncovered in TL and throughout the lipocalin family. Cation-π interactions, such as the highly conserved Trp17-Arg118 pair in TL, were educed in low temperature experiments of mutants with Trp to Tyr substitutions.
机译：阳离子-π相互作用影响蛋白质折叠，结构稳定性，特异性和分子识别。在脂质运载蛋白家族中，阳离子-π相互作用已被忽略。为了填补这一空白，在脂族蛋白家族的113种晶体和溶液结构中分析了这些相互作用。阳离子-π相互作用链接了先前确定的结构保守区域，并揭示了新的基序，这是序列比对算法无法实现的。相互作用的功能和结构意义已在人眼泪脂蛋白（TL）中进行了实验测试。 TL是一种突出的混杂脂质脂，在眼表脂质结合中起关键作用。通过枪管“开口”端处的环AB进行的配体结合调制仅被错误地归因于静电相互作用。数据显示，Phe28-Lys108对中的环间阳离子-π相互作用显着有助于稳定环AB的整体构象。在TL和整个lipocalin家族中均未发现大量能量上重要且保守的阳离子-n相互作用。阳离子-π相互作用，例如在TL中高度保守的Trp17-Arg118对，是在用Trp替代Tyr的突变体的低温实验中产生的。

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