4erq: Difference between revisions

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[[Image:4erq.jpg|left|200px]]


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==X-ray structure of WDR5-MLL2 Win motif peptide binary complex==
The line below this paragraph, containing "STRUCTURE_4erq", creates the "Structure Box" on the page.
<StructureSection load='4erq' size='340' side='right'caption='[[4erq]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[4erq]] is a 6 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=4ERQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ERQ 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]] 1.906&#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=4erq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erq OCA], [https://pdbe.org/4erq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4erq RCSB], [https://www.ebi.ac.uk/pdbsum/4erq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4erq ProSAT]</span></td></tr>
{{STRUCTURE_4erq|  PDB=4erq  |  SCENE=  }}
</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>  


===X-ray structure of WDR5-MLL2 Win motif peptide binary complex===
==See Also==
 
*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
 
== References ==
==About this Structure==
<references/>
[[4erq]] is a 6 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=4ERQ OCA].
__TOC__
[[Category: Histone-lysine N-methyltransferase]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Cosgrove, M S.]]
[[Category: Large Structures]]
[[Category: Dharmarajan, V.]]
[[Category: Cosgrove MS]]
[[Category: Lee, J H.]]
[[Category: Dharmarajan V]]
[[Category: Patel, A.]]
[[Category: Lee J-H]]
[[Category: Skalnik, D G.]]
[[Category: Patel A]]
[[Category: 3-10 helix]]
[[Category: Skalnik DG]]
[[Category: Ash2l]]
[[Category: Beta propeller]]
[[Category: Core complex]]
[[Category: Histone]]
[[Category: Lysine methyltransferase]]
[[Category: Mll1]]
[[Category: Rbbp5]]
[[Category: Transcription-transferase complex]]
[[Category: Wd40]]
[[Category: Win motif peptide]]

Latest revision as of 14:05, 1 March 2024

X-ray structure of WDR5-MLL2 Win motif peptide binary complexX-ray structure of WDR5-MLL2 Win motif peptide binary complex

Structural highlights

4erq is a 6 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 1.906Å
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

4erq, resolution 1.91Å

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