2xl2: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
m Protected "2xl2" [edit=sysop:move=sysop]
No edit summary
Line 1: Line 1:
[[Image:2xl2.png|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2xl2", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2xl2|  PDB=2xl2  |  SCENE=  }}  
{{STRUCTURE_2xl2|  PDB=2xl2  |  SCENE=  }}  
===WDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE RECRUITED TO NOVEL SITE===
===WDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE RECRUITED TO NOVEL SITE===
{{ABSTRACT_PUBMED_20716525}}


 
==Function==
<!--
[[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.
The line below this paragraph, {{ABSTRACT_PUBMED_20716525}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 20716525 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_20716525}}


==About this Structure==
==About this Structure==
Line 22: Line 10:


==Reference==
==Reference==
<ref group="xtra">PMID:020716525</ref><references group="xtra"/>
<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 11:16, 2 May 2013

Template:STRUCTURE 2xl2

WDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE RECRUITED TO NOVEL SITEWDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE RECRUITED TO NOVEL SITE

Template:ABSTRACT PUBMED 20716525

FunctionFunction

[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 StructureAbout this Structure

2xl2 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2xl2&oldid=1787970"