Systemic Amyloidoses

Supplemental Material

Video 1    This morph animation shows the transition among three unique dimer orientations present in the crystal structures of κI O18/O8 and AL-09, as well as the nuclear magnetic resonance structure of κI Y87H, to demonstrate the structural differences between them. This animation does not represent genuine conformational changes. The residues in monomer A involved in the κI dimer interface are in magenta, whereas residues outside the dimer interface are in cyan. Monomer B (ribbons) of AL-09 (blue, PDB code: 2Q1E), κI O18/O8 (gold, PDB code: 2Q20), and κI Y87H (red, PDB code: 2KQM) shows a ∼90° and ∼180° rotation with respect to the monomer A from the canonical dimer interface. In yellow ribbon are shown the differences in dimer structures, like the hands on a clock moving in intervals of 90°. Interface residues Q3, Y36, F98, and Q100 (red sticks) show the biggest conformational differences between dimer interfaces.