In human cells, Protein Arginine Deiminase 2 (PAD2) modifies chromatin state by turning arginine residues within Histone H3 N-terminal tails into citrulline. This allows chromatin to acquire the transcriptionally active, decompressed euchromatin state. In order to understand how the PAD2 active site interacts with its Histone H3 targets, PAD2 will be crystallized in complex with the N-terminal tail of Histone H3. PAD2 will be expressed and purified as a hexahistidine (6xHis) fusion protein from an <i>E. coli</i> source. 6xHis-PAD2 will be purified using affinity and size exclusion chromatography. PAD2 will be co-crystallized with Histone H3 N-terminal peptides using the hanging drop vapor diffusion method. The X-ray diffraction data will be collected and processed to generate an atomic-level model of the PAD2/Histone H3 N-terminus interaction. The PAD2/Histone H3 contacts identified from this model will be validated with mutagenesis and citrullination activity assays.

Structural characterization of protein arginine deiminase 2 interaction with histone H3 N-terminus

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