Ontology highlight
ABSTRACT:
SUBMITTER: Song JJ
PROVIDER: S-EPMC2596411 | biostudies-literature | 2008 Dec
REPOSITORIES: biostudies-literature
Song Ji-Joon JJ Kingston Robert E RE
The Journal of biological chemistry 20081007 50
WDR5 is a component of the mixed lineage leukemia (MLL) complex, which methylates lysine 4 of histone H3, and was identified as a methylated Lys-4 histone H3-binding protein. Here, we present a crystal structure of WDR5 bound to an MLL peptide. Surprisingly, we find that WDR5 utilizes the same pocket shown to bind histone H3 for this MLL interaction. Furthermore, the WDR5-MLL interaction is disrupted preferentially by mono- and di-methylated Lys-4 histone H3 over unmodified and tri-methylated Ly ...[more]