2gnq
From Proteopedia
Structure of wdr5
Overview
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.
About this Structure
2GNQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Sun May 4 05:19:03 2008
Categories: Homo sapiens | Single protein | Allali-Hassani, A. | Arrowsmith, C H. | Bochkarev, A. | Edwards, A M. | Loppnau, P. | Min, J. | Plotnikov, A N. | SGC, Structural Genomics Consortium. | Schuetz, A. | Sundstrom, M. | Vedadi, M. | Weigelt, J. | H3k4me2 binding protein | Sgc | Structural genomic | Structural genomics consortium
