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Structure of UHRF1 in complex with histone tail ; site_id, AC6 ; Number of Residues, 4 ; Details, BINDING SITE FOR RESIDUE ZN B The structure reveals that the intermodule linker plays an essential role in the formation of a histone H3-binding hole between the reader. 3ask: Image gallery including assembly, Pfam SCOP and CATH domains, ligands and environments.
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Asymmetric Unit. The histone H3 tail fits into the hole by adopting a compact fold harboring a central helix, which allows both of the reader modules to simultaneously recognize the modification states at H3-R2 and H3-K9. Plays an important role in the correlation of histone modification and gene silencing in cancer progression. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. View more in-depth experimental data.