FIG. 2. Structure of the oxidized CLIC1 dimer. A, stereo
backbone of the CLIC1 dimer; green, A subunit; red, B subunit.
In the A subunit every 10th residue is labeled. B, electron
density of the intramolecular disulfide bond between Cys-24 and
Cys-59 contoured at 1 . The CLIC1 dimer is
viewed along (C) and perpendicular (D) to the pseudo 2-fold
axis; are shown helices, A subunit (red) and B subunit (green),
and intramolecular disulfide bonds (yellow). E, ClustalW (24)
alignment of the CLIC family. The secondary structure is shown
for both monomeric (red, helices; yellow, -strands) and dimeric
(blue, helices) forms. Conserved regions are shaded; green,
putative transmembrane regions; yellow, Cys; cream, Gly.
Features unique to CLIC1 are in blue. Ramachandran distances
(see "Experimental Procedures") for the monomer to dimer
transition are plotted above its sequence. Figures were made
with SETOR (25), MOLSCRIPT (26), RASTER3D (27), and CONSCRIPT