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人类 NR-RTK 网络枢纽的结构分析。

Structural analysis of hubs in human NR-RTK network.

机构信息

Molecular and Cellular Diagnosis Processes, Centre of Biotechnology of Sfax, University of Sfax, Route Sidi Mansour, Po Box 1177, 3018 Sfax, Tunisia.

出版信息

Biol Direct. 2011 Oct 5;6:49. doi: 10.1186/1745-6150-6-49.

DOI:10.1186/1745-6150-6-49
PMID:21974810
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3220635/
Abstract

BACKGROUND

Currently a huge amount of protein-protein interaction data is available therefore extracting meaningful ones are a challenging task. In a protein-protein interaction network, hubs are considered as key proteins maintaining function and stability of the network. Therefore, studying protein-protein complexes from a structural perspective provides valuable information for predicted interactions.

RESULTS

In this study, we have predicted by comparative modelling and docking methods protein-protein complexes of hubs of human NR-RTK network inferred from our earlier study. We found that some interactions are mutually excluded while others could occur simultaneously. This study revealed by structural analysis the key role played by Estrogen receptor (ESR1) in mediating the signal transduction between human Receptor Tyrosine kinases (RTKs) and nuclear receptors (NRs).

CONCLUSIONS

Although the methods require human intervention and judgment, they can identify the interactions that could occur together or ones that are mutually exclusive. This adds a fourth dimension to interaction network, that of time, and can assist in obtaining concrete predictions consistent with experiments.

摘要

背景

目前有大量的蛋白质-蛋白质相互作用数据,因此提取有意义的相互作用是一项具有挑战性的任务。在蛋白质-蛋白质相互作用网络中,枢纽被认为是维持网络功能和稳定性的关键蛋白质。因此,从结构角度研究蛋白质-蛋白质复合物为预测相互作用提供了有价值的信息。

结果

在这项研究中,我们通过比较建模和对接方法预测了从我们之前的研究中推断出的人类 NR-RTK 网络枢纽的蛋白质-蛋白质复合物。我们发现一些相互作用是相互排斥的,而另一些相互作用则可以同时发生。这项研究通过结构分析揭示了雌激素受体(ESR1)在介导人类受体酪氨酸激酶(RTKs)和核受体(NRs)之间的信号转导中所起的关键作用。

结论

尽管这些方法需要人为干预和判断,但它们可以识别可能同时发生或相互排斥的相互作用。这为相互作用网络增加了第四个维度,即时间维度,并有助于获得与实验一致的具体预测。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/7880960a35d8/1745-6150-6-49-8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/7099ab652c0c/1745-6150-6-49-1.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/bac529916911/1745-6150-6-49-5.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/30cd56762401/1745-6150-6-49-7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/7880960a35d8/1745-6150-6-49-8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/7099ab652c0c/1745-6150-6-49-1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/28eaab7feb1c/1745-6150-6-49-2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/4361cb7f94d3/1745-6150-6-49-3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/ad859f7b3f77/1745-6150-6-49-4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/bac529916911/1745-6150-6-49-5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/f295fe63d7fb/1745-6150-6-49-6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/30cd56762401/1745-6150-6-49-7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/711b/3220635/7880960a35d8/1745-6150-6-49-8.jpg

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