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This finding implies that the intermodule linker plays an essential as a functional switch of central helix, 3ask allows both the reader modules by making extended contacts with 3zsk tandem at H3-R2 and H3-K9.

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Structure of UHRF1 in complex with histone tail ; Descriptor, E3 ubiquitin-protein ligase UHRF1, Histone H, ZINC ION, (4 entities in total) ; Functional. 3ask: Image gallery including assembly, Pfam SCOP and CATH domains, ligands and environments. Structure of UHRF1 in complex with histone tail. Help. ENTITY. 3ASK_1. E3 ubiquitin-protein ligase UHRF1 - Homo sapiens. CHROMOSOME. NC_ NC_ 5'.
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Our structural and biochemical data provide the basis for combinatorial readout of unmodified Arg-2 H3-R2 and methylated Lys-9 H3-K9 by the tandem tudor domain and the PHD finger. Homo sapiens. Views Article Discussion Edit this page History. The structure reveals that the intermodule linker plays an essential role in the formation of a histone H3-binding hole between the reader modules by making extended contacts with the tandem tudor domain. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications.