Figure 5.
FIGURE 5. Heparin oligosaccharide bound to Robo IG1-2. A,
cartoon representation of the crystallographically independent
Robo IG1-2 molecules A and B in the monoclinic crystal form. IG1
and IG2 are shown in orange and green, respectively. The bound
heparin oligosaccharide is shown in ball-and-stick
representation, with carbon atoms colored cyan. The C atoms of
basic residues implicated in heparin binding are indicated by
blue spheres. The side chains of Lys-69 and Arg-117 are defined
by the electron density, whereas those of Lys-121 and Lys-123
are disordered (see text). B, another view of the bound heparin
oligosaccharide, in an orientation roughly perpendicular to that
of panel A. Heparin binding residues are labeled. C, stereo view
of an unbiased simulated annealing omit map contoured at 2.4
,
with the final model of the heparin tetrasaccharide superimposed
on the map. D, superposition of the heparin oligosaccharides
observed in different protein-heparin co-crystal structures:
red, Robo IG1-2 (this study); purple, FGF2-FGFR1 complex (33);
green, FGF1-FGFR2 complex (31); pink, hepatocyte growth
factor/scatter factor NK1 fragment (36).
atoms of
basic residues implicated in heparin binding are indicated by
blue spheres. The side chains of Lys-69 and Arg-117 are defined
by the electron density, whereas those of Lys-121 and Lys-123
are disordered (see text). B, another view of the bound heparin
oligosaccharide, in an orientation roughly perpendicular to that
of panel A. Heparin binding residues are labeled. C, stereo view
of an unbiased simulated annealing omit map contoured at 2.4
,
with the final model of the heparin tetrasaccharide superimposed
on the map. D, superposition of the heparin oligosaccharides
observed in different protein-heparin co-crystal structures:
red, Robo IG1-2 (this study); purple, FGF2-FGFR1 complex (33);
green, FGF1-FGFR2 complex (31); pink, hepatocyte growth
factor/scatter factor NK1 fragment (36).