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| | ==Structure of the human MSL3 chromo-barrel domain at 2.5 Angstrom resolution== | | ==Structure of the human MSL3 chromo-barrel domain at 2.5 Angstrom resolution== |
| - | <StructureSection load='3ob9' size='340' side='right' caption='[[3ob9]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3ob9' size='340' side='right'caption='[[3ob9]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ob9]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OB9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OB9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ob9]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OB9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hCG_401190, MSL3, MSL3L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ob9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ob9 OCA], [http://pdbe.org/3ob9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ob9 RCSB], [http://www.ebi.ac.uk/pdbsum/3ob9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ob9 ProSAT]</span></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=3ob9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ob9 OCA], [https://pdbe.org/3ob9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ob9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ob9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ob9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Ferhatoglu, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Moore, S A]] | + | [[Category: Ferhatoglu Y]] |
| - | [[Category: Chromo]] | + | [[Category: Moore SA]] |
| - | [[Category: Chromo-barrel]]
| + | |
| - | [[Category: Chromodomain]]
| + | |
| - | [[Category: Histone h4k20me1]]
| + | |
| - | [[Category: Histone tail]]
| + | |
| - | [[Category: Methyllysine binding]]
| + | |
| - | [[Category: Nucleosome recognition]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Transcription regulator]]
| + | |
| 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]
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
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