2h9m
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WDR5 in complex with unmodified H3K4 peptide
OverviewOverview
Histone methylation at specific lysine residues brings about various, downstream events that are mediated by different effector proteins. The, WD40 domain of WDR5 represents a new class of histone methyl-lysine, recognition domains that is important for recruiting H3K4, methyltransferases to K4-dimethylated histone H3 tail as well as for, global and gene-specific K4 trimethylation. Here we report the crystal, structures of full-length WDR5, WDR5Delta23 and its complexes with, unmodified, mono-, di- and trimethylated histone H3K4 peptides. The, structures reveal that WDR5 is able to bind all of these histone H3, peptides, but only H3K4me2 peptide forms extra interactions with WDR5 by, use of both water-mediated hydrogen bonding and the altered hydrophilicity, of the modified lysine 4. We propose a mechanism for the involvement of, WDR5 in binding and presenting histone H3K4 for further methylation as a, component of MLL complexes.
DiseaseDisease
Known disease associated with this structure: Asphyxiating thoracic dystrophy OMIM:[611177]
About this StructureAbout this Structure
2H9M is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for molecular recognition and presentation of histone H3 by WDR5., Schuetz A, Allali-Hassani A, Martin F, Loppnau P, Vedadi M, Bochkarev A, Plotnikov AN, Arrowsmith CH, Min J, EMBO J. 2006 Sep 20;25(18):4245-52. Epub 2006 Aug 31. PMID:16946699
Page seeded by OCA on Mon Nov 12 22:28:48 2007