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WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket.

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 Lys-4 histone H3. These data implicate a delicate interplay between the effector, WDR5, the catalytic subunit, MLL, and the substrate, histone H3, of the MLL complex. We suggest that the activity of the MLL complex might be regulated through this interplay.

Pubmed ID: 18840606


  • Song JJ
  • Kingston RE


The Journal of biological chemistry

Publication Data

December 12, 2008

Associated Grants

  • Agency: NIBIB NIH HHS, Id: P30 EB009998

Mesh Terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Catalytic Domain
  • Crystallography, X-Ray
  • Histone-Lysine N-Methyltransferase
  • Histones
  • Humans
  • Kinetics
  • Methylation
  • Molecular Sequence Data
  • Myeloid-Lymphoid Leukemia Protein
  • Protein Binding
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Surface Plasmon Resonance