Peregrin: Difference between revisions

The PZP domain of BRPF1 is located at its N-terminus and has been shown to <scene name='91/910741/Pzp_with_h3/2'>associate with the histone H3 tail</scene> <ref name="Klein" />. Three residues in the H3 peptide undergo unique interactions with the binding pocket. These are <scene name='91/910741/H3_ala_1/1'>Ala-1</scene>, <scene name='91/910741/Arg_2/1'>Arg-2</scene>, and <scene name='91/910741/Thr-3/1'>Thr-3</scene>.<ref name="Klein" />. In addition to its binding to the histone H3 N-terminus, the PZP domain can associate non-specifically with DNA. It is thought that this interaction is mediated by lys-383, lys-390, and arg-392<ref name="Klein" />. These residues form a <scene name='91/910741/Positive_patch_pzp/1'>positively charged patch</scene> in the second PHD finger that can interact with the negative DNA backbone. Interestingly, the DNA- and histone H3-binding capabilities of the PZP domain seem to work in tandem, as is associates much stronger with the nucleosome core particle than it does with the H3 tail alone<ref name="Klein_2015">PMID:26626149</ref>.