Large-scale survey and database of high affinity ligands for peptide recognition modules
Details
Publication Year 2020,Volume 16,Issue #12,Page e9310
Journal Title
Molecular Systems Biology
Publication Type
Journal Article
Abstract
Many proteins involved in signal transduction contain peptide recognition modules (PRMs) that recognize short linear motifs (SLiMs) within their interaction partners. Here, we used large-scale peptide-phage display methods to derive optimal ligands for 163 unique PRMs representing 79 distinct structural families. We combined the new data with previous data that we collected for the large SH3, PDZ, and WW domain families to assemble a database containing 7,984 unique peptide ligands for 500 PRMs representing 82 structural families. For 74 PRMs, we acquired enough new data to map the specificity profiles in detail and derived position weight matrices and binding specificity logos based on multiple peptide ligands. These analyses showed that optimal peptide ligands resembled peptides observed in existing structures of PRM-ligand complexes, indicating that a large majority of the phage-derived peptides are likely to target natural peptide-binding sites and could thus act as inhibitors of natural protein–protein interactions. The complete dataset has been assembled in an online database (http://www.prm-db.org) that will enable many structural, functional, and biological studies of PRMs and SLiMs. © 2020 The Authors. Published under the terms of the CC BY 4.0 license
Publisher
EMBO Press
Keywords
domain specificity; peptide inhibitors; peptide library; peptide recognition modules; phage display
Research Division(s)
Inflammation
PubMed ID
33438817
Open Access at Publisher's Site
https://doi.org/10.15252/msb.20199310
Terms of Use/Rights Notice
Refer to copyright notice on published article.


Creation Date: 2021-02-01 12:08:36
Last Modified: 2021-03-02 02:41:34
An error has occurred. This application may no longer respond until reloaded. Reload 🗙