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3uvn

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Crystal structure of WDR5 in complex with the WDR5-interacting motif of SET1A

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 ==Crystal structure of WDR5 in complex with the WDR5-interacting motif of SET1A==
-<StructureSection load='3uvn' size='340' side='right' caption='[[3uvn]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
+<StructureSection load='3uvn' size='340' side='right'caption='[[3uvn]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3uvn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UVN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UVN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3uvn]] 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=3UVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UVN FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3uvk|3uvk]], [[3uvl|3uvl]], [[3uvm|3uvm]], [[3uvo|3uvo]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.792&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WDR5, BIG3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3uvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uvn OCA], [https://pdbe.org/3uvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uvn RCSB], [https://www.ebi.ac.uk/pdbsum/3uvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uvn ProSAT]</span></td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr>
+</table>
-<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=3uvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uvn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uvn RCSB], [http://www.ebi.ac.uk/pdbsum/3uvn PDBsum]</span></td></tr>
+== Function ==
-<table>
+[https://www.uniprot.org/uniprot/SET1A_HUMAN SET1A_HUMAN] Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overalpping localization with SETD1B suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression.<ref>PMID:12670868</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-In mammals, the SET1 family of lysine methyltransferases (KMTs), which includes MLL1-5, SET1A and SET1B, catalyzes the methylation of lysine-4 (Lys-4) on histone H3. Recent reports have demonstrated that a three-subunit complex composed of WD-repeat protein-5 (WDR5), retinoblastoma-binding protein-5 (RbBP5) and absent, small, homeotic disks-2-like (ASH2L) stimulates the methyltransferase activity of MLL1. On the basis of studies showing that this stimulation is in part controlled by an interaction between WDR5 and a small region located in close proximity of the MLL1 catalytic domain [referred to as the WDR5-interacting motif (Win)], it has been suggested that WDR5 might play an analogous role in scaffolding the other SET1 complexes. We herein provide biochemical and structural evidence showing that WDR5 binds the Win motifs of MLL2-4, SET1A and SET1B. Comparative analysis of WDR5-Win complexes reveals that binding of the Win motifs is achieved by the plasticity of WDR5 peptidyl-arginine-binding cleft allowing the C-terminal ends of the Win motifs to be maintained in structurally divergent conformations. Consistently, enzymatic assays reveal that WDR5 plays an important role in the optimal stimulation of MLL2-4, SET1A and SET1B methyltransferase activity by the RbBP5-ASH2L heterodimer. Overall, our findings illustrate the function of WDR5 in scaffolding the SET1 family of KMTs and further emphasize on the important role of WDR5 in regulating global histone H3 Lys-4 methylation.
-The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases.,Zhang P, Lee H, Brunzelle JS, Couture JF Nucleic Acids Res. 2012 Jan 20. PMID:22266653<ref>PMID:22266653</ref>
-From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Histone-lysine N-methyltransferase]]
 [[Category: Homo sapiens]]
-[[Category: Brunzelle, J S.]]
+[[Category: Large Structures]]
-[[Category: Couture, J F.]]
+[[Category: Brunzelle JS]]
-[[Category: Lee, H.]]
+[[Category: Couture J-F]]
-[[Category: Zhang, P.]]
+[[Category: Lee H]]
-[[Category: Beta-propeller]]
+[[Category: Zhang P]]
-[[Category: Chromatin biology]]
-[[Category: Histone h3]]
-[[Category: Nucleus]]
-[[Category: Scaffolding]]
-[[Category: Transcription]]
-[[Category: Trithorax]]

3uvn

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Crystal structure of WDR5 in complex with the WDR5-interacting motif of SET1A

Structural highlights

Function

See Also

References

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