2xl2: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xl2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xl2 RCSB], [http://www.ebi.ac.uk/pdbsum/2xl2 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xl2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xl2 RCSB], [http://www.ebi.ac.uk/pdbsum/2xl2 PDBsum]</span></td></tr> | ||
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== 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 20:57, 24 December 2014
WDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE RECRUITED TO NOVEL SITEWDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE RECRUITED TO NOVEL SITE
Structural highlights
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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHistone modification is well established as a fundamental mechanism driving the regulation of transcription, replication and DNA repair through the control of chromatin structure. Likewise, it is apparent that incorrect targeting of histone modifications contributes to misregulated gene expression and hence to developmental disorders and diseases of genomic instability such as cancer. The KMT2 family of SET domain methyltransferases, typified by MLL1, are responsible for histone H3 lysine-4 methylation, a marker of active genes. To ensure that this modification is correctly targeted, a multi-protein complex associates with the methyltransferase and directs activity. We have identified a novel interaction site on the core complex protein WDR5, and mapped the complementary site on its partner RbBP5. We have characterised this interaction by X-ray crystallography and show how it is fundamental to the assembly of the complex and to the regulation of methyltransferase activity. We show which region of RbBP5 contributes directly to MLL activation and combine our structural and biochemical data to produce a model to show how WDR5 and RbBP5 act cooperatively to stimulate activity. Characterisation of a novel WDR5 binding site that recruits RbBP5 through a conserved motif and enhances methylation of H3K4 by MLL1.,Odho Z, Southall SM, Wilson JR J Biol Chem. 2010 Aug 17. PMID:20716525[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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