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3oa6

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Template:STRUCTURE 3oa6

Contents

Human MSL3 Chromodomain bound to DNA and H4K20me1 peptide

Template:ABSTRACT PUBMED 20657587

Function

[MS3L1_HUMAN] May be involved in chromatin remodeling and transcriptional regulation. May have a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex.[1] [2] [3] [4]

About this Structure

3oa6 is a 7 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 3m9p. Full crystallographic information is available from OCA.

Reference

  • Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S. Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain. Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. Epub 2010 Jul 25. PMID:20657587 doi:10.1038/nsmb.1856
  1. ↑ Smith ER, Cayrou C, Huang R, Lane WS, Cote J, Lucchesi JC. A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. Mol Cell Biol. 2005 Nov;25(21):9175-88. PMID:16227571 doi:10.1128/MCB.25.21.9175-9188.2005
  2. ↑ Cai Y, Jin J, Swanson SK, Cole MD, Choi SH, Florens L, Washburn MP, Conaway JW, Conaway RC. Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J Biol Chem. 2010 Feb 12;285(7):4268-72. doi: 10.1074/jbc.C109.087981. Epub 2009 , Dec 14. PMID:20018852 doi:10.1074/jbc.C109.087981
  3. ↑ Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S. Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain. Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. Epub 2010 Jul 25. PMID:20657587 doi:10.1038/nsmb.1856
  4. ↑ Moore SA, Ferhatoglu Y, Jia Y, Al-Jiab RA, Scott MJ. 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. J Biol Chem. 2010 Dec 24;285(52):40879-90. doi: 10.1074/jbc.M110.134312. Epub, 2010 Oct 12. PMID:20943666 doi:10.1074/jbc.M110.134312

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