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4esg

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(New page: '''Unreleased structure''' The entry 4esg is ON HOLD Authors: Dharmarajan, Venkatasubramanian, Lee, Jeong-Heon, Patel, Anamika, Skalnik, David G., Cosgrove, Michael S. Description: X-r...)
Current revision (11:05, 1 March 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4esg is ON HOLD
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==X-ray structure of WDR5-MLL1 Win motif peptide binary complex==
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<StructureSection load='4esg' size='340' side='right'caption='[[4esg]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4esg]] 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=4ESG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ESG 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]] 1.7&#8491;</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=4esg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4esg OCA], [https://pdbe.org/4esg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4esg RCSB], [https://www.ebi.ac.uk/pdbsum/4esg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4esg ProSAT]</span></td></tr>
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</table>
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== Function ==
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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>
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Authors: Dharmarajan, Venkatasubramanian, Lee, Jeong-Heon, Patel, Anamika, Skalnik, David G., Cosgrove, Michael S.
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==See Also==
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*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
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Description: X-ray structure of WDR5-MLL1 Win motif peptide binary complex
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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: Cosgrove MS]]
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[[Category: Dharmarajan V]]
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[[Category: Lee J-H]]
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[[Category: Patel A]]
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[[Category: Skalnik DG]]

Current revision

X-ray structure of WDR5-MLL1 Win motif peptide binary complex

PDB ID 4esg

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