Structural and Biochemical Studies on the Chromo-barrel Domain of Male Specific Lethal 3 (MSL3) Reveal a Binding Preference for Mono- or Dimethyllysine 20 on Histone H4

We have determined the human male specific lethal 3 (hMSL3) chromo-barrel domain structure by x-ray crystallography to a resolution of 2.5 Å (r = 0.226, Rfree = 0.270). hMSL3 contains a canonical methyllysine binding pocket made up of residues Tyr-31, Phe-56, Trp-59, and Trp-63. A six-residue insert...

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Veröffentlicht in:	The Journal of biological chemistry 2010-12, Vol.285 (52), p.40879-40890
Hauptverfasser:	Moore, Stanley A., Ferhatoglu, Yurdagul, Jia, Yunhua, Al-Jiab, Rami A., Scott, Maxwell J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Animals Animals, Genetically Modified Binding Sites Chromatin Chromatin Regulation Chromo-barrel Domain Chromosomal Proteins, Non-Histone Crystal Structure DNA-Binding Proteins Drosophila Drosophila Dosage Compensation Drosophila melanogaster Drosophila Proteins - chemistry Drosophila Proteins - genetics Drosophila Proteins - metabolism Epigenetics Female Gene Regulation H4K20 Histone Methylation Histones - chemistry Histones - genetics Histones - metabolism Humans Male MRG15 MSL3 Mutation, Missense Nuclear Proteins - chemistry Nuclear Proteins - genetics Nuclear Proteins - metabolism Protein Binding Structure-Activity Relationship Transcription Factors - chemistry Transcription Factors - genetics Transcription Factors - metabolism
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