Figure 2.
Figure 2. Stereo view of interacting residues in the PAI-1 -SMB
interface. (a) The region of the somatomedin B domain that
interacts with PAI-1 overlaps extensively with that involved in
the interaction with uPAR, as alanine-scanning mutagenesis has
shown that residues Asp22, Glu23, Leu24, Tyr27 and Tyr28 of
vitronectin (highlighted with magenta bonds) are important for
the interaction with uPAR16. Somatomedin B coloring ranges from
blue at the N terminus to red at the C terminus. (b) Electron
density from the final [A]-weighted^26
map showing the interaction between helix F (hF) of PAI-1 (gray
bonds) and the loop comprising residues 23 -28 of SMB (pink
bonds). The map is contoured at a level of 1.25 the
r.m.s. electron density. For clarity, contours >2 Å from an atom
in the figure are omitted.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2003,
10,
541-544)
copyright 2003.
[A]-weighted^26
map showing the interaction between helix F (hF) of PAI-1 (gray
bonds) and the loop comprising residues 23 -28 of SMB (pink
bonds). The map is contoured at a level of 1.25 
the
r.m.s. electron density. For clarity, contours >2 Å from an atom
in the figure are omitted.