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4ery
From Proteopedia
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==X-ray structure of WDR5-MLL3 Win motif peptide binary complex== | ==X-ray structure of WDR5-MLL3 Win motif peptide binary complex== | ||
| - | <StructureSection load='4ery' size='340' side='right' caption='[[4ery]], [[Resolution|resolution]] 1.30Å' scene=''> | + | <StructureSection load='4ery' size='340' side='right'caption='[[4ery]], [[Resolution|resolution]] 1.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4ery]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4ery]] is a 2 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=4ERY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ERY FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</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=4ery FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ery OCA], [https://pdbe.org/4ery PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ery RCSB], [https://www.ebi.ac.uk/pdbsum/4ery PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ery ProSAT]</span></td></tr> | |
| - | <tr | + | </table> |
| - | + | == Function == | |
| - | <table> | + | [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> |
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| + | ==See Also== | ||
| + | *[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Cosgrove | + | [[Category: Large Structures]] |
| - | [[Category: Dharmarajan | + | [[Category: Cosgrove MS]] |
| - | [[Category: Lee | + | [[Category: Dharmarajan V]] |
| - | [[Category: Patel | + | [[Category: Lee J-H]] |
| - | [[Category: Skalnik | + | [[Category: Patel A]] |
| - | + | [[Category: Skalnik DG]] | |
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Current revision
X-ray structure of WDR5-MLL3 Win motif peptide binary complex
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