Author(s)

Yali Zhang, YuyunWu, Hongying Yang, Shuhui Yu, Li Zhao, Yingbin Yang

Corresponding Author

Yali Zhang

Abstract

In order to investigate the occurrence of cis-peptide bond, the study counted the incidence of different cis-peptide bonds from a non-redundant data set containing 1591 protein PDBs. Then, 20 different amino acid residues were used to replace β -catenin S246 residues and transferred into HepG2 cells and observed the variation of the storage of different mutants in the nucleus and the interaction with APC. The results showed that the cis-peptide bond of 82.30% (703/854) was distributed in XP X is an arbitrary amino acid residue, P is a proline residue) site of the protein polypeptide chain, and different cis-peptide The incidence of different, which when X is tyrosine, tryptophan and other residues XP has the highest incidence of cis-peptide Bond; and X is leucine, methionine and other residues XP has the lowest results of the interaction between APC and β-catenin was weak when S246 mutated into tyrosine and tryptophan residues, and the interaction of APC with β-catenin was weak. When S246 mutates into leucine and methionine residues, the interaction between APC and β-catenin is relatively enhanced. It is suggested that the change of β-catenin function is related to the change of cis-peptide bond In the X246P site. The results of this study are expected to provide new strategies for genetic disease prediction, genetic diagnosis, and protein modification.

Keywords

Cis-Peptide Bond, Incidence, Β-Catenin, Nuclear Accumulation.