1. Nat. Rev. Rheumatol. doi:10.1038/nrrheum.2017.132
Figure 2 Protein citrullination catalysed by human peptidylarginine deiminases
Figure 2 | Protein citrullination catalysed by human peptidylarginine deiminases. a | In human peptidylarginine deiminase (PAD)2 and PAD4, a ∼375 residue calcium dependent α/β propeller catalytic domain is preceded by two IgG domains. The substrate interacts with the main chain of the reactive site cleft on both sides of the deiminated arginine side chain (indicated by red lines), while the arginine guanidine group interacts with the catalytic residues (Asp350 and Asp473). b | Human PADs catalyse the hydrolytic, calcium-dependent conversion of arginine residues within a polypeptide chain to citrulline residues, releasing ammonia in the process.
Potempa, J. et al. (2017) The case for periodontitis in the pathogenesis of rheumatoid arthritis
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