PDZ12串联中配体依赖的结构域内和结构域间运动调节突触后密度蛋白-95的结合界面

IF 3 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY FEBS Letters Pub Date : 2020-03-01 DOI:10.1002/1873-3468.13626
Bertalan Kovács, Nóra Zajácz-Epresi, Zoltán Gáspári
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引用次数: 7

摘要

突触后密度蛋白-95(PSD-95)通过其肽结合PDZ结构域介导的相互作用调节突触可塑性。PSD‐95的两个N末端PDZ结构域形成一个自主结构单元,其结构域间取向和动力学取决于配体结合。为了理解配体结合效应的机制细节,我们使用可用的实验确定的核Overhauser效应原子间距离和S2阶参数生成了构象系综。在我们的方法中,两个领域的快速动力学是独立处理的。我们发现配体结合诱导的结构域内结构变化调节了特定结构域-结构域取向发生的概率。我们的结果表明,PDZ结构域中的β2-β3环是一个关键的调控区,它影响结构域内运动和超分子重排。
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Ligand‐dependent intra‐ and interdomain motions in the PDZ12 tandem regulate binding interfaces in postsynaptic density protein‐95
The postsynaptic density protein‐95 (PSD‐95) regulates synaptic plasticity through interactions mediated by its peptide‐binding PDZ domains. The two N‐terminal PDZ domains of PSD‐95 form an autonomous structural unit, and their interdomain orientation and dynamics depend on ligand binding. To understand the mechanistic details of the effect of ligand binding, we generated conformational ensembles using available experimentally determined nuclear Overhauser effect interatomic distances and S2 order parameters. In our approach, the fast dynamics of the two domains is treated independently. We find that intradomain structural changes induced by ligand binding modulate the probability of the occurrence of specific domain–domain orientations. Our results suggest that the β2‐β3 loop in the PDZ domains is a key regulatory region, which influences both intradomain motions and supramodular rearrangement.
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来源期刊
FEBS Letters
FEBS Letters 生物-生化与分子生物学
CiteScore
6.60
自引率
2.90%
发文量
303
审稿时长
1 months
期刊介绍: FEBS Letters is one of the world''s leading journals in molecular biology and is renowned both for its quality of content and speed of production. Bringing together the most important developments in the molecular biosciences, FEBS Letters provides an international forum for Minireviews, Research Letters and Hypotheses that merit urgent publication.
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