Proteomics

Dataset Information

0

A simple method for developing lysine targeted covalent protein reagents


ABSTRACT: In this project we developed phosphopeptides functionalized with methacrylate ester warheads installed on a cysteine residue, which bind covalently to the protein 14-3-3 sigma. We prepared complexes of the purified protein with the peptides and used trypsin digestion and LC-MSMS to elucidate the binding site of the peptides, by comparison of compound-treated complexes to DMSO-treated protein and observing the disappearance on non-modified peptides. The file names are based on internal names used for the project and are distinct from the names given to the peptides in the final publication. Names are as follows: 4IEA - peptide 3 in the final publication 128C - peptide 8 in the final publication 132C - peptide 11 in the final publication

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Ronen Gabizon  

LAB HEAD: Nir London

PROVIDER: PXD044257 | Pride | 2024-01-26

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
14-3-3128C1.raw Raw
14-3-3128C1_PRM.raw Raw
14-3-3128C2.raw Raw
14-3-3128C2_PRM.raw Raw
14-3-3128C3.raw Raw
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Publications

A simple method for developing lysine targeted covalent protein reagents.

Gabizon Ronen R   Tivon Barr B   Reddi Rambabu N RN   van den Oetelaar Maxime C M MCM   Amartely Hadar H   Cossar Peter J PJ   Ottmann Christian C   London Nir N  

Nature communications 20231201 1


Peptide-based covalent probes can target shallow protein surfaces not typically addressable using small molecules, yet there is a need for versatile approaches to convert native peptide sequences into covalent binders that can target a broad range of residues. Here we report protein-based thio-methacrylate esters-electrophiles that can be installed easily on unprotected peptides and proteins via cysteine side chains, and react efficiently and selectively with cysteine and lysine side chains on t  ...[more]

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