4z4p: Difference between revisions
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<StructureSection load='4z4p' size='340' side='right'caption='[[4z4p]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='4z4p' size='340' side='right'caption='[[4z4p]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4z4p]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4z4p]] is a 1 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=4Z4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z4P FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <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=4z4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z4p OCA], [https://pdbe.org/4z4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z4p RCSB], [https://www.ebi.ac.uk/pdbsum/4z4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z4p ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Disease == | == Disease == | ||
[ | [https://www.uniprot.org/uniprot/KMT2D_HUMAN KMT2D_HUMAN] Kabuki syndrome. The disease is caused by mutations affecting the gene represented in this entry. | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/KMT2D_HUMAN KMT2D_HUMAN] Histone methyltransferase. Methylates 'Lys-4' of histone H3 (H3K4me). H3K4me represents a specific tag for epigenetic transcriptional activation. Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription.<ref>PMID:16603732</ref> <ref>PMID:17500065</ref> <ref>PMID:17851529</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Histone methyltransferase|Histone methyltransferase]] | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gamblin | [[Category: Gamblin SJ]] | ||
[[Category: Mittal | [[Category: Mittal A]] | ||
[[Category: Reich | [[Category: Reich S]] | ||
[[Category: Reid | [[Category: Reid J]] | ||
[[Category: Wilson | [[Category: Wilson JR]] | ||
[[Category: Zhang | [[Category: Zhang Z]] | ||
Latest revision as of 13:57, 10 January 2024
Structure of the MLL4 SET DomainStructure of the MLL4 SET Domain
Structural highlights
DiseaseKMT2D_HUMAN Kabuki syndrome. The disease is caused by mutations affecting the gene represented in this entry. FunctionKMT2D_HUMAN Histone methyltransferase. Methylates 'Lys-4' of histone H3 (H3K4me). H3K4me represents a specific tag for epigenetic transcriptional activation. Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription.[1] [2] [3] Publication Abstract from PubMedMethylation of histone H3 lysine-4 is a hallmark of chromatin associated with active gene expression. The activity of H3K4-specific modification enzymes, in higher eukaryotes the MLL (or KMT2) family, is tightly regulated. The MLL family has six members, each with a specialized function. All contain a catalytic SET domain that associates with a core multiprotein complex for activation. These SET domains segregate into three classes that correlate with the arrangement of targeting domains that populate the rest of the protein. Here we show that, unlike MLL1, the MLL4 SET domain retains significant activity without the core complex. We also present the crystal structure of an inactive MLL4-tagged SET domain construct and describe conformational changes that account for MLL4 intrinsic activity. Finally, our structure explains how the MLL SET domains are able to add multiple methyl groups to the target lysine, despite having the sequence characteristics of a classical monomethylase. Evolving Catalytic Properties of the MLL Family SET Domain.,Zhang Y, Mittal A, Reid J, Reich S, Gamblin SJ, Wilson JR Structure. 2015 Aug 27. pii: S0969-2126(15)00324-X. doi:, 10.1016/j.str.2015.07.018. PMID:26320581[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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