2XL2
WDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE RECRUITED TO NOVEL SITE
Summary for 2XL2
| Entry DOI | 10.2210/pdb2xl2/pdb |
| Related | 2XL3 |
| Descriptor | WD REPEAT-CONTAINING PROTEIN 5, RETINOBLASTOMA-BINDING PROTEIN 5, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | transcription, mll complex, h3k4 methylation, wd-40 beta-propeller |
| Biological source | MUS MUSCULUS (MOUSE) More |
| Cellular location | Nucleus (By similarity): P61965 Q8BX09 |
| Total number of polymer chains | 4 |
| Total formula weight | 76722.30 |
| Authors | Odho, Z.,Southall, S.M.,Wilson, J.R. (deposition date: 2010-07-19, release date: 2010-08-04, Last modification date: 2023-12-20) |
| Primary citation | Odho, Z.,Southall, S.M.,Wilson, J.R. Characterisation of a Novel Wdr5 Binding Site that Recruits Rbbp5 Through a Conserved Motif and Enhances Methylation of H3K4 by Mll1. J.Biol.Chem., 285:32967-, 2010 Cited by PubMed Abstract: 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 mixed lineage leukemia protein-1 (MLL1), is responsible for histone H3 lysine 4 methylation, a marker of active genes. To ensure that this modification is correctly targeted, a multiprotein complex associates with the methyltransferase and directs activity. We have identified a novel interaction site on the core complex protein WD repeat protein-5 (WDR5), and we mapped the complementary site on its partner retinoblastoma-binding protein-5 (RbBP5). We have characterized 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 mixed lineage leukemia activation, and we combine our structural and biochemical data to produce a model to show how WDR5 and RbBP5 act cooperatively to stimulate activity. PubMed: 20716525DOI: 10.1074/JBC.M110.159921 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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