Fig. 2

Domain structure and functions of DFS70/LEDGF and its splice variant p52. The two variants share a common amino (N)-terminal region (amino acids 1–325) comprised by a PWWP domain, a nuclear localization signal (NLS), two AT-hook DNA binding domains, and three charged regions (CR). The carboxyl (C)-terminal region of DFS70/LEDGF (amino acids 326–530) is absent in p52 and contains the HIV integrase binding domain (IBD), which overlaps with the autoepitope region recognized by the anti-DFS autoantibodies. The extreme C-terminal region of p52 contains a short intron-derived sequence (amino acids 325–333) not present in DFS70/LEDGF designated carboxy-terminal tail (CTT). The known functions of the N- and C-terminal regions are listed