Link to bioRxiv paper:

http://biorxiv.org/cgi/content/short/2020.07.24.217752v1?rss=1

Authors: Fan, Y., Wang, X., Wang, C.

Abstract:

14-3-3s present in multiple isoforms in human cells and mediate signal transduction by binding to phosphoserine-containing proteins. Recent findings have demonstrated that 14-3-3s act as a key factor in promoting chemoresistance of cancer. Here, we aimed to develop the predictive models that can determine the binding affinity of phosphopeptide fragments against 14-3-3s. It is found that the hydrophobic property of residues in phosphopeptides has a significant contribution to the binding affinity for most of 14-3-3 isoforms. The conserved patterns of 14-3-3 biding motifs were verified by our predictions. A group of peptide sequences were predicted with high binding affinity and high sequence conservation, which had agreement with 14-3-3s ligands. Overall, our results demonstrate that how the residues are likely to function in 14-3-3s interaction and the computational methods we introduced may contribute to the further research.

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