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3UVM

Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL4

Summary for 3UVM
Entry DOI10.2210/pdb3uvm/pdb
Related3UVK 3UVL 3UVN 3UVO
DescriptorWD repeat-containing protein 5, Histone-lysine N-methyltransferase MLL4 (3 entities in total)
Functional Keywordstrithorax, chromatin biology, beta-propeller, scaffolding, histone h3, nucleus, transcription
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus: P61964
Nucleus (By similarity): Q9UMN6
Total number of polymer chains2
Total formula weight35901.71
Authors
Zhang, P.,Lee, H.,Brunzelle, J.S.,Couture, J.-F. (deposition date: 2011-11-30, release date: 2011-12-14, Last modification date: 2023-09-13)
Primary citationZhang, P.,Lee, H.,Brunzelle, J.S.,Couture, J.F.
The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases.
Nucleic Acids Res., 40:4237-4246, 2012
Cited by
PubMed: 22266653
DOI: 10.1093/nar/gkr1235
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.57 Å)
Structure validation

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