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==Crystal structure of WDR5, WD repeat domain 5 in complex with compound SGC-DS-MT-0345==
==Crystal structure of WDR5, WD repeat domain 5 in complex with compound SGC-DS-MT-0345==
<StructureSection load='4qqe' size='340' side='right' caption='[[4qqe]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='4qqe' size='340' side='right'caption='[[4qqe]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4qqe]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QQE FirstGlance]. <br>
<table><tr><td colspan='2'>[[4qqe]] 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=4QQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QQE FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=37F:N-[2-(4-METHYLPIPERAZIN-1-YL)-5-(QUINOLIN-3-YL)PHENYL]-6-OXO-4-(TRIFLUOROMETHYL)-1,6-DIHYDROPYRIDINE-3-CARBOXAMIDE'>37F</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qqe RCSB], [http://www.ebi.ac.uk/pdbsum/4qqe PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=37F:N-[2-(4-METHYLPIPERAZIN-1-YL)-5-(QUINOLIN-3-YL)PHENYL]-6-OXO-4-(TRIFLUOROMETHYL)-1,6-DIHYDROPYRIDINE-3-CARBOXAMIDE'>37F</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
<table>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqe OCA], [https://pdbe.org/4qqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qqe RCSB], [https://www.ebi.ac.uk/pdbsum/4qqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qqe ProSAT]</span></td></tr>
</table>
== Function ==
[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>
 
==See Also==
*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Al-Awar, R.]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C H.]]
[[Category: Large Structures]]
[[Category: Bountra, C.]]
[[Category: Al-Awar R]]
[[Category: Brown, P J.]]
[[Category: Arrowsmith CH]]
[[Category: Dombrovski, L.]]
[[Category: Bountra C]]
[[Category: Dong, A.]]
[[Category: Brown PJ]]
[[Category: Edwards, A M.]]
[[Category: Dombrovski L]]
[[Category: Getlik, M.]]
[[Category: Dong A]]
[[Category: Poda, G.]]
[[Category: Edwards AM]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Getlik M]]
[[Category: Schapira, M.]]
[[Category: Poda G]]
[[Category: Senisterra, G.]]
[[Category: Schapira M]]
[[Category: Smil, D.]]
[[Category: Senisterra G]]
[[Category: Vedadi, M.]]
[[Category: Smil D]]
[[Category: Wernimont, A.]]
[[Category: Vedadi M]]
[[Category: Wu, H.]]
[[Category: Wernimont A]]
[[Category: Sgc]]
[[Category: Wu H]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]
[[Category: Transcription]]
[[Category: Wdr5]]

Latest revision as of 20:35, 20 September 2023

Crystal structure of WDR5, WD repeat domain 5 in complex with compound SGC-DS-MT-0345Crystal structure of WDR5, WD repeat domain 5 in complex with compound SGC-DS-MT-0345

Structural highlights

4qqe is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3] [4] [5]

See Also

References

  1. ↑ Patel A, Dharmarajan V, Vought VE, Cosgrove MS. On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J Biol Chem. 2009 Sep 4;284(36):24242-56. Epub 2009 Jun 25. PMID:19556245 doi:M109.014498
  2. ↑ Guelman S, Kozuka K, Mao Y, Pham V, Solloway MJ, Wang J, Wu J, Lill JR, Zha J. The double-histone-acetyltransferase complex ATAC is essential for mammalian development. Mol Cell Biol. 2009 Mar;29(5):1176-88. doi: 10.1128/MCB.01599-08. Epub 2008 Dec, 22. PMID:19103755 doi:10.1128/MCB.01599-08
  3. ↑ Cai Y, Jin J, Swanson SK, Cole MD, Choi SH, Florens L, Washburn MP, Conaway JW, Conaway RC. Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J Biol Chem. 2010 Feb 12;285(7):4268-72. doi: 10.1074/jbc.C109.087981. Epub 2009 , Dec 14. PMID:20018852 doi:10.1074/jbc.C109.087981
  4. ↑ Han Z, Guo L, Wang H, Shen Y, Deng XW, Chai J. Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5. Mol Cell. 2006 Apr 7;22(1):137-44. PMID:16600877 doi:10.1016/j.molcel.2006.03.018
  5. ↑ Couture JF, Collazo E, Trievel RC. Molecular recognition of histone H3 by the WD40 protein WDR5. Nat Struct Mol Biol. 2006 Aug;13(8):698-703. Epub 2006 Jul 9. PMID:16829960 doi:10.1038/nsmb1116

4qqe, resolution 1.80Å

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