3M9Q
Drosophila MSL3 chromodomain
Summary for 3M9Q
Entry DOI | 10.2210/pdb3m9q/pdb |
Related | 3M9P |
Descriptor | Protein male-specific lethal-3 (2 entities in total) |
Functional Keywords | chromodomain, msl3, methyllysine recognition, aromatic cage, msl complex, transcription upregulation, dna binding protein |
Biological source | Drosophila melanogaster (Fruit fly) |
Cellular location | Nucleus : P50536 |
Total number of polymer chains | 2 |
Total formula weight | 24562.10 |
Authors | Kim, D.,Huang, P.,Rastinejad, F.,Khorasanizadeh, S. (deposition date: 2010-03-22, release date: 2010-07-21, Last modification date: 2023-09-06) |
Primary citation | Kim, D.,Blus, B.J.,Chandra, V.,Huang, P.,Rastinejad, F.,Khorasanizadeh, S. Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain. Nat.Struct.Mol.Biol., 17:1027-1029, 2010 Cited by PubMed Abstract: MSL3 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. PubMed: 20657587DOI: 10.1038/nsmb.1856 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.29 Å) |
Structure validation
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