Figure 1.
FIG. 1. Structure of gankyrin. A, stereo view of the 2F[o]
- F[c] electron density maps contoured at the 1 level
and displayed on residues 74-78 of ANK2 and 107-111 of ANK3.
B-D, orthogonal ribbon representations of gankyrin. The
polypeptide chain is color-ramped from its N terminus in blue to
the C terminus in red. E, alignment of the five full ankyrin
repeat sequences (ANK1-ANK5) together with sequences at the N
(ANK0) and C (ANK6) termini of the molecule, which in the
structure adopts the ankyrin repeat fold. The schematic below
the alignment indicates the span of the -helical and -strand
segments of the structure. A consensus ankyrin repeat sequence
(16) is shown below the structure. Residues that match the
consensus are in blue. F, van der Waals surface representation
of gankyrin, with residues colored according to side chain
polarity: white, apolar; green, neutral polar; red, acidic;
blue, basic. The view is of the concave surface of the molecule
in the same orientation as in D.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2004,
279,
1541-1545)
copyright 2004.
level
and displayed on residues 74-78 of ANK2 and 107-111 of ANK3.
B-D, orthogonal ribbon representations of gankyrin. The
polypeptide chain is color-ramped from its N terminus in blue to
the C terminus in red. E, alignment of the five full ankyrin
repeat sequences (ANK1-ANK5) together with sequences at the N
(ANK0) and C (ANK6) termini of the molecule, which in the
structure adopts the ankyrin repeat fold. The schematic below
the alignment indicates the span of the 
-helical and 
-strand
segments of the structure. A consensus ankyrin repeat sequence
(16) is shown below the structure. Residues that match the
consensus are in blue. F, van der Waals surface representation
of gankyrin, with residues colored according to side chain
polarity: white, apolar; green, neutral polar; red, acidic;
blue, basic. The view is of the concave surface of the molecule
in the same orientation as in D.