This protein is a unique member of Fpg/NEIL family of DNA glysosylases which shows preference for both oxidative purines and pyrimidine lesions. Originally identified through in-silico studies from Wallace, Mitra and Seeger group back in 2002, the crystallisation of NEIL3 remained challenge for almost a decade due to the difficulty in getting fulll length purification of the protein as it tend to aggregate until a trancated version was crystallised in 2013 and the crystal structure publlished.

Neil3 proteins are almost twice the size of other Fpg/Nei family members. The N terminus of the Neil3 proteins is highly conserved, with a complete Fpg/Nei-like core protein that harbors an H2TH motif and a canonical zinc finger motif. Neil3 proteins also have a Ran binding protein (RanBP2)-type zinc finger motif and a duplicated GRF-zinc finger motif at their extended C terminus (Bandaru et al., 2002; Krokeide et al., 2009; Liu et al., 2010; Morland et al., 2002; Takao et al., 2009; Torisu et al., 2005)

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Function

== Disease

Relevance

Structural highlights

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