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Figure 1.
Fig. 1. The crystal structures of bH1 Fab bound to HER2 or
VEGF. (A) The bH1 Fab (gray)/HER2 (gold) superimposed on to the
Herceptin (pink)/HER2 (red) complex (left), and bH1 Fab (light
blue)/VEGF (green, teal) complex (right). (B) Fab surface
residues are colored according to the extent buried in the
complex (red, >75%; orange, >50 to 75%; yellow, >25 to 50%). The
underlined amino acids differ between bH1 and Herceptin. The
white dotted line separates the LC and HC. (C) Superposition of
the CDR loops of VEGF and HER2-bound bH1 (blue, gray) and
HER2-bound Herceptin (pink) in the same orientation as in (B).
(D) CDR-L1 regions of the two bH1 complexes shown in the same
orientation. The residues with temperature factors higher than
average are shown in red and orange. VEGF would clash with Tyr32
of bH1 in its HER2-bound conformation.
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