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| | <StructureSection load='2y0n' size='340' side='right'caption='[[2y0n]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='2y0n' size='340' side='right'caption='[[2y0n]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2y0n]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y0N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2y0n]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y0N FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y0n OCA], [https://pdbe.org/2y0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y0n RCSB], [https://www.ebi.ac.uk/pdbsum/2y0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y0n ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y0n OCA], [https://pdbe.org/2y0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y0n RCSB], [https://www.ebi.ac.uk/pdbsum/2y0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y0n ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MS3L1_HUMAN 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.<ref>PMID:16227571</ref> <ref>PMID:20018852</ref> <ref>PMID:20657587</ref> <ref>PMID:20943666</ref>
| + | [https://www.uniprot.org/uniprot/MS3L1_HUMAN 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.<ref>PMID:16227571</ref> <ref>PMID:20018852</ref> <ref>PMID:20657587</ref> <ref>PMID:20943666</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Akhtar, A]] | + | [[Category: Akhtar A]] |
| - | [[Category: Cusack, S]] | + | [[Category: Cusack S]] |
| - | [[Category: Hallacli, E]] | + | [[Category: Hallacli E]] |
| - | [[Category: Holz, H]] | + | [[Category: Holz H]] |
| - | [[Category: Kadlec, J]] | + | [[Category: Kadlec J]] |
| - | [[Category: Lipp, M]] | + | [[Category: Lipp M]] |
| - | [[Category: Weatherby, J Sanchez]] | + | [[Category: Sanchez Weatherby J]] |
| - | [[Category: Chromatin]]
| + | |
| - | [[Category: Msl complex]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: X chromosome]]
| + | |
| Structural highlights
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]
Publication Abstract from PubMed
The male-specific lethal (MSL) complex is required for dosage compensation in Drosophila melanogaster, and analogous complexes exist in mammals. We report structures of binary complexes of mammalian MSL3 and the histone acetyltransferase (HAT) MOF with consecutive segments of MSL1. MSL1 interacts with MSL3 as an extended chain forming an extensive hydrophobic interface, whereas the MSL1-MOF interface involves electrostatic interactions between the HAT domain and a long helix of MSL1. This structure provides insights into the catalytic mechanism of MOF and enables us to show analogous interactions of MOF with NSL1. In Drosophila, selective disruption of Msl1 interactions with Msl3 or Mof severely affects Msl1 targeting to the body of dosage-compensated genes and several high-affinity sites, without affecting promoter binding. We propose that Msl1 acts as a scaffold for MSL complex assembly to achieve specific targeting to the X chromosome.
Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1.,Kadlec J, Hallacli E, Lipp M, Holz H, Sanchez-Weatherby J, Cusack S, Akhtar A Nat Struct Mol Biol. 2011 Feb;18(2):142-9. Epub 2011 Jan 9. PMID:21217699[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Kadlec J, Hallacli E, Lipp M, Holz H, Sanchez-Weatherby J, Cusack S, Akhtar A. Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1. Nat Struct Mol Biol. 2011 Feb;18(2):142-9. Epub 2011 Jan 9. PMID:21217699 doi:10.1038/nsmb.1960
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