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Figure 4.
Figure 4. Stereo View of Ligand Cα TracesLigands were
superimposed using the Cα atoms of core residues (see text).
The Cα traces have been rotated 55° about a horizontal axis
relative to Figure 5 and are as follows: TGFα molecules C (red
with yellow disulfide bonds) and D (blue) from this study;
minimized average NMR structure of TGFα (orange) from PDB:2TGF
(Harvey et al., 1991); diphtheria toxin bound heparin binding
EGF (gray) from PDB:1XDT (Louie et al., 1997); and crystallized
human EGF molecule A (purple) and molecule B (green) from
PDB:1JL9 (Lu et al., 2001). While the two TGFα molecules from
this study (C and D), EGF molecule A of 1JL9, and hbEGF
superimpose well from residue 14, the top half of the B loop
adopts different conformations in the NMR structure (2TGF) and
1JL9:B (top of each panel). In the uncomplexed form, the N
terminus of TGFα is structurally heterogeneous (bottom left of
each panel).
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