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4cy2

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<StructureSection load='4cy2' size='340' side='right'caption='[[4cy2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4cy2' size='340' side='right'caption='[[4cy2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4cy2]] is a 3 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=4CY2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CY2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4cy2]] is a 3 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=4CY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CY2 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cy1|4cy1]], [[4cy3|4cy3]], [[4cy5|4cy5]]</td></tr>
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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]] 2&#8491;</td></tr>
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<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=4cy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cy2 OCA], [http://pdbe.org/4cy2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cy2 RCSB], [http://www.ebi.ac.uk/pdbsum/4cy2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cy2 ProSAT]</span></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=4cy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cy2 OCA], [https://pdbe.org/4cy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cy2 RCSB], [https://www.ebi.ac.uk/pdbsum/4cy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cy2 ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[http://www.uniprot.org/uniprot/KANL1_HUMAN KANL1_HUMAN]] 17q21.31 microdeletion syndrome;Koolen-De Vries syndrome due to a point mutation.
 
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/WDR5_HUMAN WDR5_HUMAN]] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.<ref>PMID:19556245</ref> <ref>PMID:19103755</ref> <ref>PMID:20018852</ref> <ref>PMID:16600877</ref> <ref>PMID:16829960</ref> [[http://www.uniprot.org/uniprot/KANL1_HUMAN KANL1_HUMAN]] As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription.<ref>PMID:20018852</ref> <ref>PMID:22547026</ref> [[http://www.uniprot.org/uniprot/KANL2_HUMAN KANL2_HUMAN]] As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription.<ref>PMID:20018852</ref>
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[https://www.uniprot.org/uniprot/WDR5_HUMAN WDR5_HUMAN] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.<ref>PMID:19556245</ref> <ref>PMID:19103755</ref> <ref>PMID:20018852</ref> <ref>PMID:16600877</ref> <ref>PMID:16829960</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==
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*[[WD repeat-containing protein|WD repeat-containing protein]]
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*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Brettschneider, J]]
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[[Category: Brettschneider J]]
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[[Category: Cusack, S]]
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[[Category: Cusack S]]
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[[Category: Dias, J]]
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[[Category: Dias J]]
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[[Category: Kadlec, J]]
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[[Category: Kadlec J]]
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[[Category: Chromatin]]
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[[Category: Epigenetic regulator]]
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[[Category: Histone acetylation]]
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[[Category: Transcription]]
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Current revision

Crystal structure of the KANSL1-WDR5-KANSL2 complex.

PDB ID 4cy2

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