ArticleJournal of the American Chemical Society2011
Biophysical probes reveal a "compromise" nature of the methyl-lysine binding pocket in L3MBTL1.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 33 citations in OpenAlex.
- Chemical tools targeting readers of lysine methylation.Current opinion in chemical biology · 2023Review
- L3MBTL3 is induced by HIF-1α and fine tunes the HIF-1α degradation under hypoxia in vitro.Heliyon · 2023Article
- Targeting protein methylation: from chemical tools to precision medicines.Cellular and molecular life sciences : CMLS · 2019Review
- Chemical and Biochemical Perspectives of Protein Lysine Methylation.Chemical reviews · 2018Review
- Select human cancer mutants of NRMT1 alter its catalytic activity and decrease N-terminal trimethylation.Protein science : a publication of the Protein Society · 2017Article
- Design, synthesis, and protein methyltransferase activity of a unique set of constrained amine containing compounds.Bioorganic & medicinal chemistry letters · 2016Article
- Chemical probes for methyl lysine reader domains.Current opinion in chemical biology · 2016Review
- The L3MBTL3 Methyl-Lysine Reader Domain Functions As a Dimer.ACS chemical biology · 2016Article
- Selective Inhibition of CBX6: A Methyllysine Reader Protein in the Polycomb Family.ACS medicinal chemistry letters · 2016Article
- Molecular Insights into Inhibition of the Methylated Histone-Plant Homeodomain Complexes by Calixarenes.The Journal of biological chemistry · 2015Article
- Inhibition of histone binding by supramolecular hosts.The Biochemical journal · 2014Article
- Discovery of a chemical probe for the L3MBTL3 methyllysine reader domain.Nature chemical biology · 2013Article
- Assessment of free energy predictors for ligand binding to a methyllysine histone code reader.Journal of computational chemistry · 2012Article
- Drug discovery toward antagonists of methyl-lysine binding proteins.Current chemical genomics · 2011Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Histone lysine methylation (Kme) encodes essential information modulating many biological processes including gene expression and transcriptional regulation. However, the atomic-level recognition mechanisms of methylated histones by their respective adaptor proteins are still elusive. For instance, it is unclear how L3MBTL1, a methyl-lysine histone code reader, recognizes equally well both mono- and dimethyl marks but ignores unmodified and trimethylated lysine residues. We made use of molecular dynamics (MD) and free energy perturbation (FEP) techniques in order to investigate the energetics and dynamics of the methyl-lysine recognition. Isothermal titration calorimetry (ITC) was employed to experimentally validate the computational findings. Both computational and experimental methods were applied to a set of designed "biophysical" probes that mimic the shape of a single lysine residue and reproduce the binding affinities of cognate histone peptides. Our results suggest that, besides forming favorable interactions, the L3MBTL1 binding pocket energetically penalizes both methylation states and has most probably evolved as a "compromise" that nonoptimally fits to both mono- and dimethyl-lysine marks.
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