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Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader†
Yan-Jiun Lee,M. J. Schmidt,Jeffery M. Tharp,Annemarie Weber,Amber L. Koenig,Hong Zheng,Jianmin Gao,Marcey L. Waters,Daniel Summerer,Wenshe R. Liu
Chemical Communications Pub Date : 09/27/2016 00:00:00 , DOI:10.1039/C6CC05959G
Abstract

Fluorophenylalanines bearing 2–5 fluorine atoms at the phenyl ring have been genetically encoded by amber codon. Replacement of F59, a phenylalanine residue that is directly involved in interactions with trimethylated K9 of histone H3, in the Mpp8 chromodomain recombinantly with fluorophenylalanines significantly impairs the binding to a K9-trimethylated H3 peptide.

Graphical abstract: Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader
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