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Figure 5.
FIGURE 5. Common hot spot of VEGF for binding of VEGFR1,
G6, and B20-4. Depicted is the surface of VEGF. All residues
that form contacts with VEGFR1, G6, and B20-4 are colored
yellow, and all residues that when exchanged to alanine cause a
loss in binding affinity of >4-fold in all three complexes are
colored red. All residues that differ in the sequence between
mouse and human VEGF are green. Only 5 of the 10 residues that
differ in the receptor binding domain of human and murine VEGF
are labeled; the remaining 5 residues are disordered in the
crystal structure of the VEGF or more distant from the binding
interface of the molecules investigated here.
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