Figure 2.
FIGURE 2. Structure-based sequence alignment of the six
ankyrin repeats of TRPV2. A, a consensus ankyrin repeat sequence
(16) is shown at the top, with designating a non-polar
residue and x any residue. -Helices are red and
3[10] helices blue. Residues identical to consensus counterparts
are boxed gray, showing a high level of conservation of a
glycine at the second position and aliphatic residues in the
inner and outer helices. The numbers in the last column are the
lengths of inner/outer helices. B, superposition of repeats
1–4 of TRPV2-ARD (gold) and ankyrin (red, 1N11 (27); repeats
16–21 shown) highlights the large twist between repeats 4 and
5 of TRPV2-ARD.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
25006-25010)
copyright 2006.
designating a non-polar
residue and x any residue. 
-Helices are red and
3[10] helices blue. Residues identical to consensus counterparts
are boxed gray, showing a high level of conservation of a
glycine at the second position and aliphatic residues in the
inner and outer helices. The numbers in the last column are the
lengths of inner/outer helices. B, superposition of repeats
1–4 of TRPV2-ARD (gold) and ankyrin (red, 1N11 (27); repeats
16–21 shown) highlights the large twist between repeats 4 and
5 of TRPV2-ARD.