Homology modeling of the wild-type and mutant Pax2 paired domain-DNA complex.

<p>The paired domain of wild-type Pax2 domain DNA are represented by red and white ribbons, respectively, and their corresponding atomic structures are shown by red and white bonds (A). Hydrogen bonds are shown in blue. Threonine 74 in the mouse protein sequence (equivalent to T75A in human) is absolutely conserved across several species (B) and across all known murine Pax-family members (C). Fragments of the Pax2 paired domain–DNA complex modified by the mutations T74A, dup73ET and G75S are shown on (D–F), respectively. Hydrogen bonds presented in the wild type protein that are broken by the mutation T74A are labeled as 1 and 2 for (D) and by the mutation G75S is labeled as 3 (F). Yellow arrows indicate the location of mutations in Pax2 paired domain. A schematic of the Pax2b protein modified from Lechner <i>et al. </i><a href="http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1000870#pgen.1000870-Lechner1" target="_blank">[32]</a> showing the paired domain (gray), the octapeptide (Oct) domain (yellow), and the C-terminus, which is rich in proline, serine, threonine and tyrosine (PSTY) residues (G). Numbers indicate amino acid position. The arrow denotes the approximate position of the three mutations studied.