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Figure 1.
Fig. 1. 3D NMR structure of ECD1–CRF-R2  in
complex with astressin. (A) Superposition of 20 energy-minimized
conformers representing the 3D NMR structure of free
ECD1–CRF-R2 (the backbone C^  atoms of
residues 57–83 and 99–120 were superimposed). (B)
Superposition of 20 energy-minimized conformers of ECD1–CRF-R2
in
complex with astressin (the backbone C^ atoms of residues
57–120 of ECD1 and 30–41 of astressin were superimposed).
The backbone of residues 44–122 of ECD1 is shown in magenta,
and the backbone of residues Leu-27–Ile-41 of astressin is
colored in green. In A and B the disulfide bonds are shown in
yellow. (C) Ribbon diagram of the lowest energy conformer
representing the 3D NMR structure of the ECD–CRF-R2 –astressin complex.
The -sheets are shown in
cyan, and the side chains of the core residues Trp-71 and
Trp-109 along with the disulfide bonds are shown in yellow. The
salt bridge Arg-101 (in blue)–Asp-65 (in red) is shown as
dashed spine in orange. The backbone of astressin from
Leu-27–Ile-41 is shown in green. (D) Side view of the ribbon
diagram shown in C. MOLMOL was used to generate the figures (49).
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