4b86

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'''Unreleased structure'''
 
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The entry 4b86 is ON HOLD
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==Crystal structure of the MSL1-MSL2 complex (3.5A)==
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<StructureSection load='4b86' size='340' side='right'caption='[[4b86]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4b86]] is a 12 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=4B86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B86 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b86 OCA], [https://pdbe.org/4b86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b86 RCSB], [https://www.ebi.ac.uk/pdbsum/4b86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b86 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MSL1_HUMAN MSL1_HUMAN] Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which is implicated in the formation of higher-order chromatin structure. Greatly enhances MSL2 E3 ubiquitin ligase activity, promoting monoubiquitination of histone H2B at 'Lys-34' (H2BK34Ub). This modification in turn stimulates histone H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. In the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together for enzymatic activity regulation.<ref>PMID:16227571</ref> <ref>PMID:21726816</ref> <ref>PMID:22547026</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Male-Specific Lethal (MSL) complex regulates dosage compensation of the male X chromosome in Drosophila. Here, we report the crystal structure of its MSL1/MSL2 core, where two MSL2 subunits bind to a dimer formed by two molecules of MSL1. Analysis of structure-based mutants revealed that MSL2 can only interact with the MSL1 dimer, but MSL1 dimerization is MSL2 independent. We show that Msl1 is a substrate for Msl2 E3 ubiquitin ligase activity. ChIP experiments revealed that Msl1 dimerization is essential for targeting and spreading of the MSL complex on X-linked genes; however, Msl1 binding to promoters of male and female cells is independent of the dimer status and other MSL proteins. Finally, we show that loss of Msl1 dimerization leads to male-specific lethality. We propose that Msl1-mediated dimerization of the entire MSL complex is required for Msl2 binding, X chromosome recognition, and spreading along the X chromosome.
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Authors: Hallacli, E., Lipp, M., Georgiev, P., Spielman, C., Cusack, S., Akhtar, A., Kadlec, J.
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Msl1-mediated dimerization of the dosage compensation complex is essential for male X-chromosome regulation in Drosophila.,Hallacli E, Lipp M, Georgiev P, Spielman C, Cusack S, Akhtar A, Kadlec J Mol Cell. 2012 Nov 30;48(4):587-600. doi: 10.1016/j.molcel.2012.09.014. Epub 2012, Oct 18. PMID:23084835<ref>PMID:23084835</ref>
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Description: Crystal structure of the MSL1-MSL2 complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4b86" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Akhtar A]]
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[[Category: Cusack S]]
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[[Category: Georgiev P]]
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[[Category: Hallacli E]]
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[[Category: Kadlec J]]
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[[Category: Lipp M]]
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[[Category: Spielman C]]

Current revision

Crystal structure of the MSL1-MSL2 complex (3.5A)

PDB ID 4b86

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