2xl3

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[[Image:2xl3.png|left|200px]]
 
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{{STRUCTURE_2xl3| PDB=2xl3 | SCENE= }}
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===WDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE AND HISTONE H3 PEPTIDE===
===WDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE AND HISTONE H3 PEPTIDE===
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{{ABSTRACT_PUBMED_20716525}}
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==Function==
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[[http://www.uniprot.org/uniprot/RBBP5_MOUSE RBBP5_MOUSE]] As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid. Does not affect ES cell self-renewal.
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{{ABSTRACT_PUBMED_20716525}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:020716525</ref><references group="xtra"/>
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<ref group="xtra">PMID:020716525</ref><references group="xtra"/><references/>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Odho, Z.]]
[[Category: Odho, Z.]]

Revision as of 08:17, 2 May 2013

Template:STRUCTURE 2xl3

Contents

WDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE AND HISTONE H3 PEPTIDE

Template:ABSTRACT PUBMED 20716525

Function

[RBBP5_MOUSE] As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid. Does not affect ES cell self-renewal.

About this Structure

2xl3 is a 6 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

  • Odho Z, Southall SM, Wilson JR. Characterisation of a novel WDR5 binding site that recruits RbBP5 through a conserved motif and enhances methylation of H3K4 by MLL1. J Biol Chem. 2010 Aug 17. PMID:20716525 doi:10.1074/jbc.M110.159921

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OCA

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