Department of Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy.
Laboratoire de Biologie Computationnelle et Quantitative (LCQB) - UMR 7238, Sorbonne Université, Univ P6, CNRS, IBPS, Paris, France.
Immunogenetics. 2020 Apr;72(3):155-164. doi: 10.1007/s00251-020-01155-9. Epub 2020 Feb 10.
S100A7 has been suggested to interact with Ran-binding protein 9. Both proteins are nowadays considered key effectors in immune response. Functional interaction between proteins is ensured by coevolution. The mechanisms of vertebrate coevolution between S100A7 and RanBP9 remain unclear. Several approaches for studying coevolution have been developed. Protein coevolution was inferred by calculating the linear correlation coefficients between inter-protein distance matrices using Mirrortree. We found an overall moderate correlation value (R = 0.53, p < 1e-06). Moreover, owing to the high conservation of RanBP9 protein among vertebrates, we chose to utilize a recent version of Blocks in Sequences (BIS2) algorithm implemented in BIS2Analyzer webserver. A coevolution cluster was identified between the two proteins (p < 8.10e-05). In conclusion, our coevolutionary analysis suggests that amino acid variations may modulate S100A7/RanBP9 interaction with potential pathogenic effects. Such findings could guide further analysis to better elucidate the function of S100A7 and RanBP9 and to design drugs targeting for these molecules in diseases.
S100A7 已被证实与 Ran 结合蛋白 9 相互作用。这两种蛋白现在被认为是免疫反应的关键效应因子。蛋白间的功能相互作用由共进化所保证。脊椎动物 S100A7 和 RanBP9 之间共进化的机制尚不清楚。已经开发了几种研究共进化的方法。通过使用 Mirrortree 计算蛋白间距离矩阵的线性相关系数，推断蛋白共进化。我们发现整体相关值适中（R=0.53，p<1e-06）。此外，由于 RanBP9 蛋白在脊椎动物中高度保守，我们选择利用最近版本的 Blocks in Sequences (BIS2) 算法在 BIS2Analyzer 网络服务器中实现。两个蛋白之间确定了一个共进化簇（p<8.10e-05）。总之，我们的共进化分析表明，氨基酸变异可能调节 S100A7/RanBP9 相互作用，具有潜在的致病影响。这些发现可以指导进一步的分析，以更好地阐明 S100A7 和 RanBP9 的功能，并设计针对这些分子的疾病治疗药物。
