Publikation: Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader
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2016
Autor:innen
Lee, Yan-Jiun
Tharp, Jeffery M.
Koenig, Amber L.
Gao, Jianmin
Waters, Marcey L.
Liu, Wenshe R.
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Chemical Communications : ChemComm. 2016, 52(85), pp. 12606-12609. ISSN 0009-241X. eISSN 1364-548X. Available under: doi: 10.1039/c6cc05959g
Zusammenfassung
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.
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LEE, Yan-Jiun, Moritz J. SCHMIDT, Jeffery M. THARP, Annemarie WEBER, Amber L. KOENIG, Hong ZHENG, Jianmin GAO, Marcey L. WATERS, Daniel SUMMERER, Wenshe R. LIU, 2016. Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader. In: Chemical Communications : ChemComm. 2016, 52(85), pp. 12606-12609. ISSN 0009-241X. eISSN 1364-548X. Available under: doi: 10.1039/c6cc05959gBibTex
@article{Lee2016Genet-37676,
year={2016},
doi={10.1039/c6cc05959g},
title={Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader},
number={85},
volume={52},
issn={0009-241X},
journal={Chemical Communications : ChemComm},
pages={12606--12609},
author={Lee, Yan-Jiun and Schmidt, Moritz J. and Tharp, Jeffery M. and Weber, Annemarie and Koenig, Amber L. and Zheng, Hong and Gao, Jianmin and Waters, Marcey L. and Summerer, Daniel and Liu, Wenshe R.}
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<dcterms:abstract xml:lang="eng">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.</dcterms:abstract>
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