Figure 1.
FIGURE 1. The TRPV2-ARD structure. A, primary structure of
TRPV2. Ankyrin repeats are shown in labeled gray boxes; starred
repeats are not recognized by sequence motif searches. B, left:
Coomassie-stained gel of 2.5 µg of each of
the three final protein samples used in crystallization,
constructs 62-326, 75-321 (Se-Met substituted), and 75-321.
Right: representative size exclusion chromatography trace of
construct 75–321 on a Superdex 200 10/30 column. Arrows
indicate elution volumes of molecular mass standards (molecular
mass in kDa). C, ribbon diagram of TRPV2-ARD showing each
ankyrin repeat in a distinct color. D, superposition of
TRPV2-ARD structures. For clarity, only one chain from each
crystal form is shown. Regions showing the most variability are
colored green, gold, and blue for crystal forms I, II, and III,
respectively. E, a large number of aromatic residues (shown in
purple) are concentrated on the solvent-exposed surface of
fingers 2 and 3.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
25006-25010)
copyright 2006.
2.5 µg of each of
the three final protein samples used in crystallization,
constructs 62-326, 75-321 (Se-Met substituted), and 75-321.
Right: representative size exclusion chromatography trace of
construct 75–321 on a Superdex 200 10/30 column. Arrows
indicate elution volumes of molecular mass standards (molecular
mass in kDa). C, ribbon diagram of TRPV2-ARD showing each
ankyrin repeat in a distinct color. D, superposition of
TRPV2-ARD structures. For clarity, only one chain from each
crystal form is shown. Regions showing the most variability are
colored green, gold, and blue for crystal forms I, II, and III,
respectively. E, a large number of aromatic residues (shown in
purple) are concentrated on the solvent-exposed surface of
fingers 2 and 3.