2xl2

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

Structural highlights 2xl2 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function WDR5_MOUSE 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 (By similarity). 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 PubMed Histone 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also WD-repeat protein 3D structures

spinqualitylabelsall models 2xl2, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image