|
Figure 4.
Structure of the CRF-(27-41)-NH[2]-bound CRFR1 ECD at 3.4
Å resolution. A, ribbon diagram of the crystal form III
complex with the CRFR1 ECD colored slate blue and CRF yellow.
MBP is not shown for clarity. B, electron density maps for CRF.
The 2F[o] - F[c] omit map (blue) is contoured at 1 σ and the
F[o] - F[c] omit map (green) is contoured at 3 σ. The maps were
prepared as described under “Experimental Procedures.” C,
detail of the interface depicted as in Fig. 3D. D, alignment of
the crystal form II and form III structures. C-α backbone
traces are shown with the CRF-(22-41)-NH[2]-bound ECD colored
slate blue and CRF-(22-41)-NH[2] yellow. The
CRF-(27-41)-NH[2]-bound ECD is colored blue and
CRF-(27-41)-NH[2] sand.
|
