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Figure 1.
Fig. 1. (a)C^  plot of c-Met in
complex with K-252a. The inhibitor is green. The model extends
from residues 1050 to 1360. Disordered and not included in the
model are residues 1100-1103 (apo-Met: 1099-1103) and residues
1286-1291 (1286-1290), as well as the A-loop residues 1231-1244
in apo c-Met. Residues mutated in human cancer are highlighted
with their C^ atoms in red. (b) A
view of parts of the N lobe and the A loop. Carbonyl carbon
positions of residues mentioned in the discussion are shown as
green spheres. A is blue, Cis
orange, their flanking regions (including part of  3 that
precedes C) are yellow, and the
N-terminal portion of the A loop is red. (c) A view of the
domain interface as in b. The glycine-rich loop is blue, C is
orange, residues 1190-1221 (including the C terminus of E and
the catalytic loop) are yellow, and the A loop is red. Red
labels indicate the residues mutated in our study. (d) Surface
of c-Met:K-252a with the A loop shown as a yellow ribbon. Also
shown are parts of the bound inhibitor, as well as side chains
for Phe-1234 and Asp-1235. For comparison, the A loops in IRK0P
(blue; also shown is Y1162, PDB ID code 1IRK [PDB]
; ref. 23) and FGFRK (red; PDB ID code 1FGI [PDB]
; ref. 43) are shown. All figures were prepared by using ICM
(44).
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