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New page: '''Unreleased structure''' The entry 3oa6 is ON HOLD Authors: Kim, D., Huang, P., Rastinejad, F., Khorasanizadeh, S. Description: Human MSL3 Chromodomain bound to DNA and H4K20me1 pept... |
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==Human MSL3 Chromodomain bound to DNA and H4K20me1 peptide== | |||
<StructureSection load='3oa6' size='340' side='right' caption='[[3oa6]], [[Resolution|resolution]] 2.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3oa6]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3m9p 3m9p]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OA6 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m9q|3m9q]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSL3, MSL3L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3oa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oa6 OCA], [http://pdbe.org/3oa6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3oa6 RCSB], [http://www.ebi.ac.uk/pdbsum/3oa6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3oa6 ProSAT]</span></td></tr> | |||
</table> | |||
== 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> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/3oa6_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3oa6 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain.,Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. Epub 2010 Jul 25. PMID:20657587<ref>PMID:20657587</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3oa6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Huang, P]] | |||
[[Category: Khorasanizadeh, S]] | |||
[[Category: Kim, D]] | |||
[[Category: Rastinejad, F]] | |||
[[Category: Aromatic cage]] | |||
[[Category: Chromodomain]] | |||
[[Category: Dna]] | |||
[[Category: Dna backbone recognition]] | |||
[[Category: Dna binding protein]] | |||
[[Category: Dna binding protein-dna complex]] | |||
[[Category: H4k20me1]] | |||
[[Category: Histone h4 tail]] | |||
[[Category: Methyllysine recognition]] | |||
[[Category: Msl complex]] | |||
[[Category: Msl3]] | |||
[[Category: Transcription upregulation]] | |||
Latest revision as of 17:04, 4 August 2016
Human MSL3 Chromodomain bound to DNA and H4K20me1 peptideHuman MSL3 Chromodomain bound to DNA and H4K20me1 peptide
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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMSL3 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. Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain.,Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. Epub 2010 Jul 25. PMID:20657587[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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