3oa6
Human MSL3 Chromodomain bound to DNA and H4K20me1 peptideHuman MSL3 Chromodomain bound to DNA and H4K20me1 peptide
Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMSL3 resides in the MSL (male-specific lethal) complex, which upregulates transcription by spreading the histone H4 Lys16 (H4K16) acetyl mark. We discovered a DNA-dependent interaction of MSL3 chromodomain with the H4K20 monomethyl mark. The structure of a ternary complex shows that the DNA minor groove accommodates the histone H4 tail, and monomethyllysine inserts in a four-residue aromatic cage in MSL3. H4K16 acetylation antagonizes MSL3 binding, suggesting that MSL function is regulated by a combination of post-translational modifications. Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain.,Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. Epub 2010 Jul 25. PMID:20657587[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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