|
Figure 5.
Fig. 5. Crystal structure of the complex between Imp  (44-54) and
Imp (70-529).
A, stereoview of the electron density (drawn with the program
BOBSCRIPT (52)) in the region of the peptide bound to the major
binding site of Imp (70-529).
All peptide residues were omitted from the model and simulated
annealing run with the starting temperature of 1000 K. The
electron density map was calculated with coefficients 3|F[obs]|
 2|F[calc]|
and data between 30 and 2.8 Å resolution and contoured at
1.3 standard deviations. Superimposed is the refined model of
the peptide. B, schematic diagram of the complex. Importin- is shown as
a ribbon diagram (yellow; drawn with program RIBBONS (53)). The
superhelical axis of the repetitive part of the molecule is
approximately horizontal. The two peptides are shown in a
ball-and-stick representation; the peptide bound to the major
site is colored cyan, and the peptide bound to the minor site is
colored red. C, superposition of the Imp (44-54)
peptide (cyan) and the corresponding region of full-length
importin (magenta)
bound to the major NLS-binding site of importin- . The C
atoms of
residues 70-496 were used in the superposition (drawn with the
program RIBBONS (53)).
|
