Recognition of stapled histone H3K4me3 peptides by epigenetic reader proteins.

Autor:	Betlem P; Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands., Maas MN; Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark. mecinovic@sdu.dk., Middelburg J; Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands., Pieters BJGE; Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands., Mecinović J; Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.; Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark. mecinovic@sdu.dk.
Jazyk:	angličtina
Zdroj:	Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2022 Nov 01; Vol. 58 (87), pp. 12196-12199. Date of Electronic Publication: 2022 Nov 01.
DOI:	10.1039/d2cc04294k
Abstrakt:	The flexible N-terminal histone tails are a subject of numerous posttranslational modifications, including methylation. We report development of stapled histone peptides bearing trimethyllysine as ligands for epigenetic reader proteins. Stronger or weaker binding affinities have been observed for stapled histone peptides relative to linear histones, indicating that selectivity towards reader proteins can be achieved.
Databáze:	MEDLINE
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