Unknown

Dataset Information

0

Covalent and Noncovalent Targeting of the Tcf4/β-Catenin Strand Interface with β-Hairpin Mimics.


ABSTRACT: β-Strands are a fundamental component of protein structure, and these extended peptide regions serve as binding epitopes for numerous protein-protein complexes. However, synthetic mimics that capture the conformation of these epitopes and inhibit selected protein-protein interactions are rare. Here we describe covalent and noncovalent β-hairpin mimics of an extended strand region mediating the Tcf4/β-catenin interaction. Our efforts afford a rationally designed lead for an underexplored region of β-catenin, which has been the subject of numerous ligand discovery campaigns.

SUBMITTER: Blosser SL 

PROVIDER: S-EPMC8687824 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Covalent and Noncovalent Targeting of the Tcf4/β-Catenin Strand Interface with β-Hairpin Mimics.

Blosser Sarah L SL   Sawyer Nicholas N   Maksimovic Igor I   Ghosh Brahma B   Arora Paramjit S PS  

ACS chemical biology 20210721 8


β-Strands are a fundamental component of protein structure, and these extended peptide regions serve as binding epitopes for numerous protein-protein complexes. However, synthetic mimics that capture the conformation of these epitopes and inhibit selected protein-protein interactions are rare. Here we describe covalent and noncovalent β-hairpin mimics of an extended strand region mediating the Tcf4/β-catenin interaction. Our efforts afford a rationally designed lead for an underexplored region o  ...[more]

Similar Datasets

| S-EPMC5478005 | biostudies-literature
| S-EPMC8184503 | biostudies-literature
| S-EPMC11562385 | biostudies-literature
| S-EPMC4586640 | biostudies-literature
| S-EPMC8481668 | biostudies-literature
| S-EPMC5561724 | biostudies-literature
| S-EPMC10141592 | biostudies-literature
| S-EPMC8938628 | biostudies-literature
| S-EPMC10635039 | biostudies-literature
| S-EPMC6651286 | biostudies-literature