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Chem Commun (Camb). 2018 Mar 7;54(19):2409-2412. doi: 10.1039/c8cc01009a. Epub 2018 Feb 19.

Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins.

Author information

1
Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, Nijmegen 6525 AJ, The Netherlands. j.mecinovic@science.ru.nl.
2
Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, UK.
3
ICREA, Pg. Lluís Companys 23, Barcelona 08010, Spain and Departament de Química Inorgànica i Orgànica & IQTCUB, Universitat de Barcelona, Martí i Franquès 1-11, Barcelona 08028, Spain.
4
Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, Nijmegen 6525 AJ, The Netherlands. j.mecinovic@science.ru.nl and Department of Theoretical Chemistry and Amsterdam Center for Multiscale Modeling (ACMM), Vrije Universiteit Amsterdam, De Boelelaan 1083, Amsterdam 1081 HV, The Netherlands.

Abstract

Histone Nε-lysine methylation is a widespread posttranslational modification that is specifically recognised by a diverse class of Nε-methyllysine binding reader proteins. Combined thermodynamic data, molecular dynamics simulations, and quantum chemical studies reveal that reader proteins efficiently bind trimethylornithine and trimethylhomolysine, the simplest Nε-trimethyllysine analogues that differ in the length of the side chain.

PMID:
29457186
DOI:
10.1039/c8cc01009a
[Indexed for MEDLINE]

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