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.
MeSH terms
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics
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Epigenesis, Genetic*
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Histones / chemistry*
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Histones / genetics
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Humans
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Lysine / analogs & derivatives*
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Lysine / chemistry
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Lysine / genetics
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Lysine / metabolism
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Molecular Dynamics Simulation
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Molecular Structure
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Ornithine / analogs & derivatives
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Peptide Fragments / chemistry*
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Peptide Fragments / genetics
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Protein Binding
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Quantum Theory
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Thermodynamics
Substances
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Carrier Proteins
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Histones
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Peptide Fragments
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trimethylhomolysine
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trimethylornithine
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trimethyllysine
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Ornithine
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Lysine