Direct mapping of ligandable tyrosines and lysines in cells with chiral sulfonyl fluoride probes
Ontology highlight
ABSTRACT: Advances in chemoproteomic technology have revealed covalent interactions between small molecules and protein nucleophiles, primarily cysteine, on a proteome-wide scale. Most chemoproteomic screening approaches are indirect, relying on competition between electrophilic fragments and a minimalist electrophilic probe with inherently limited proteome coverage. Here, we develop a chemoproteomic platform for direct electrophile-site identification based on enantiomeric pairs of clickable arylsulfonyl fluoride probes. Using stereoselective site modification as a proxy for ligandability in intact cells, we identified 634 tyrosines and lysines within functionally diverse protein sites, liganded by structurally diverse probes.
INSTRUMENT(S): Orbitrap Eclipse
ORGANISM(S): Homo Sapiens (ncbitaxon:9606)
SUBMITTER: Jack Taunton
PROVIDER: MSV000090778 | MassIVE | Wed Nov 23 15:26:00 GMT 2022
REPOSITORIES: MassIVE
ACCESS DATA