4gm8

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'''Unreleased structure'''
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{{STRUCTURE_4gm8| PDB=4gm8 | SCENE= }}
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===Crystal structure of human WD repeat domain 5 with compound MM-102===
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{{ABSTRACT_PUBMED_23210835}}
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The entry 4gm8 is ON HOLD until Paper Publication
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==Function==
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[[http://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: Karatas, H., Townsend, E.C., Chen, Y., Bernard, D., Cao, F., Liu, L., Lei, M., Dou, Y., Wang, S.
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==About this Structure==
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[[4gm8]] is a 8 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=4GM8 OCA].
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Description: Crystal structure of human WD repeat domain 5 with compound MM-102
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==Reference==
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<ref group="xtra">PMID:023210835</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Bernard, D.]]
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[[Category: Cao, F.]]
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[[Category: Chen, Y.]]
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[[Category: Dou, Y.]]
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[[Category: Karatas, H.]]
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[[Category: Lei, M.]]
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[[Category: Liu, L.]]
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[[Category: Townsend, E C.]]
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[[Category: Wang, S.]]
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[[Category: Histone methyltransferase]]
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[[Category: Mll1]]
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[[Category: Transcription-transcription inhibitor complex]]
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[[Category: Wd40]]

Revision as of 05:16, 1 August 2013

Template:STRUCTURE 4gm8

Contents

Crystal structure of human WD repeat domain 5 with compound MM-102

Template:ABSTRACT PUBMED 23210835

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]

About this Structure

4gm8 is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Karatas H, Townsend EC, Cao F, Chen Y, Bernard D, Liu L, Lei M, Dou Y, Wang S. High-affinity, small-molecule peptidomimetic inhibitors of MLL1/WDR5 protein-protein interaction. J Am Chem Soc. 2013 Jan 16;135(2):669-82. doi: 10.1021/ja306028q. Epub 2012 Dec, 27. PMID:23210835 doi:10.1021/ja306028q
  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

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