Abstract
Abstract14-3-3s 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.
Publisher
Cold Spring Harbor Laboratory
Reference66 articles.
1. 14-3-3 proteins: A historic overview
2. Alastair Aitken , D. B. Collinge , B. P.H. van Heusden , T. Isobe , P. H. Roseboom , G. Rosenfeld , and J. Soll . 14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins, 1992.
3. The crystal structure of the non-liganded 14-3-3σ protein: insights into determinants of isoform specific ligand binding and dimerization
4. 14-3-3 Proteins: a Number of Functions for a Numbered Protein;Science’s STKE: signal transduction knowledge environment,2005
5. Peter Bruce and Andrew Bruce . Practical Statistics for Data Scientists: 50 Essential Concepts. “O’Reilly Media, Inc.”, 2017.