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The L3MBTL3 methyl-lysine reader domain functions as a dimer
L3MBTL3 recognizes mono- and dimethylated lysine residues on histone tails. The recently reported X-ray co-crystal structures of the chemical probe UNC1215 and inhibitor UNC2533 bound to the methyl-lysine reading MBT domains of L3MBTL3 demonstrate a unique and flexible 2:2 dimer mode of recognition....
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| Veröffentlicht in: | ACS Chem Biol |
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| Hauptverfasser: | , , , , |
| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
2015
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4775453/ https://ncbi.nlm.nih.gov/pubmed/26317848 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acschembio.5b00632 |
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