3OA6

Human MSL3 Chromodomain bound to DNA and H4K20me1 peptide

Replaces:  3M9P

Summary for 3OA6

• Entry DOI: 10.2210/pdb3oa6/pdb
• Related: 3M9Q
• Descriptor: Male-specific lethal 3 homolog, DNA (5'-D(*GP*CP*TP*AP*GP*GP*TP*CP*AP*AP*AP*GP*GP*TP*CP*A)-3'), DNA (5'-D(*CP*TP*GP*AP*CP*CP*TP*TP*TP*GP*AP*CP*CP*TP*AP*G)-3'), ... (6 entities in total)
• Functional Keywords: chromodomain, msl3, histone h4 tail, dna backbone recognition, methyllysine recognition, h4k20me1, aromatic cage, msl complex, transcription upregulation, dna binding protein-dna complex, dna binding protein, dna, dna binding protein/dna
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : Q8N5Y2
• Total number of polymer chains: 7
• Total formula weight: 48551.31

Authors

Kim, D.,Huang, P.,Rastinejad, F.,Khorasanizadeh, S. (deposition date: 2010-08-04, release date: 2010-08-18, Last modification date: 2025-03-26)

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

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: 20657587
DOI: 10.1038/nsmb.1856

Experimental method

X-RAY DIFFRACTION (2.35 Å)