4b7y: Difference between revisions

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 ==Crystal structure of the MSL1-MSL2 complex==
-<StructureSection load='4b7y' size='340' side='right' caption='[[4b7y]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
+<StructureSection load='4b7y' size='340' side='right'caption='[[4b7y]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4b7y]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buakea_kaeuae Buakea kaeuae] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B7Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B7Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4b7y]] is a 4 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=4B7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B7Y FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.25&#8491;</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=4b7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b7y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b7y RCSB], [http://www.ebi.ac.uk/pdbsum/4b7y PDBsum]</span></td></tr>
+<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b7y OCA], [https://pdbe.org/4b7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b7y RCSB], [https://www.ebi.ac.uk/pdbsum/4b7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b7y ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>  [[http://www.uniprot.org/uniprot/MSL2_HUMAN MSL2_HUMAN]] Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure. Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histine H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1.<ref>PMID:21726816</ref>
+[https://www.uniprot.org/uniprot/MSL2_HUMAN MSL2_HUMAN] Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure. Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histine H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1.<ref>PMID:21726816</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4b7y" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Buakea kaeuae]]
 [[Category: Homo sapiens]]
-[[Category: Akhtar, A]]
+[[Category: Large Structures]]
-[[Category: Cusack, S]]
+[[Category: Akhtar A]]
-[[Category: Georgiev, P]]
+[[Category: Cusack S]]
-[[Category: Hallacli, E]]
+[[Category: Georgiev P]]
-[[Category: Kadlec, J]]
+[[Category: Hallacli E]]
-[[Category: Lipp, M]]
+[[Category: Kadlec J]]
-[[Category: Spielman, C]]
+[[Category: Lipp M]]
-[[Category: Chromatin]]
+[[Category: Spielman C]]
-[[Category: Dosage compensation]]
-[[Category: Gene regulation]]