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BeAtMuSiC:预测突变对蛋白质-蛋白质结合亲和力的影响。

BeAtMuSiC: Prediction of changes in protein-protein binding affinity on mutations.

机构信息

Department of BioModelling, BioInformatics and BioProcesses, Université Libre de Bruxelles, CP165/61, Av. Fr. Roosevelt 50, 1050 Brussels, Belgium.

出版信息

Nucleic Acids Res. 2013 Jul;41(Web Server issue):W333-9. doi: 10.1093/nar/gkt450. Epub 2013 May 30.

Abstract

The ability of proteins to establish highly selective interactions with a variety of (macro)molecular partners is a crucial prerequisite to the realization of their biological functions. The availability of computational tools to evaluate the impact of mutations on protein-protein binding can therefore be valuable in a wide range of industrial and biomedical applications, and help rationalize the consequences of non-synonymous single-nucleotide polymorphisms. BeAtMuSiC (http://babylone.ulb.ac.be/beatmusic) is a coarse-grained predictor of the changes in binding free energy induced by point mutations. It relies on a set of statistical potentials derived from known protein structures, and combines the effect of the mutation on the strength of the interactions at the interface, and on the overall stability of the complex. The BeAtMuSiC server requires as input the structure of the protein-protein complex, and gives the possibility to assess rapidly all possible mutations in a protein chain or at the interface, with predictive performances that are in line with the best current methodologies.

摘要

蛋白质与各种(大分子)分子伴侣建立高度选择性相互作用的能力是实现其生物功能的关键前提。因此,提供计算工具来评估突变对蛋白质-蛋白质结合的影响,在广泛的工业和生物医学应用中可能具有价值,并有助于合理化非同义单核苷酸多态性的后果。BeAtMuSiC(http://babylone.ulb.ac.be/beatmusic)是一种粗粒度的预测工具,可预测点突变引起的结合自由能变化。它依赖于一组从已知蛋白质结构中得出的统计势,并结合了突变对界面相互作用强度以及复合物整体稳定性的影响。BeAtMuSiC 服务器需要输入蛋白质-蛋白质复合物的结构,并提供快速评估蛋白质链或界面中所有可能突变的可能性,其预测性能与当前最佳方法一致。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e58/3692068/9f21a674a978/gkt450f1p.jpg

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