Figure 5. Structural basis for RP13 disease mechanisms. (AandB) Location of human RP13-linked residues (A) and yeast RP13-like residues (B) in the structures of human and yeast Brr2^HR–Prp8^Jab1 complexes. Brr2 is shown in surface representation. RP13-linked (human) or RP13-like (yeast) residues are shown with small spheres and are labeled. Type I residues/positions, black; type II residues/positions and proximal tail, violet; type III residues/positions and distal tail, green. Other colors as before. (C) Scheme illustrating the phenotypes associated with the various types of RP13-linked/RP13-like mutations. Symbols as in Figure 3. Green arrows or “+” indicate functional processes, red lines or “-“ indicate dysfunctional processes; dashed red lines or “-/+” indicate partial functionality. Brr2 inhibition or activation by Prp8^Jab1 variants bearing type I exchanges could not be tested as the proteins were insoluble. However, type I exchanges would be expected to also severely interfere with Brr2 regulation in cases where soluble protein is produced in vivo.