Figure 3.
Figure 3. Structures of the X11 PDZ
domains determined by NMR spectroscopy. (a -c) Ribbon
diagrams of representative NMR structures of PDZ1 (a), PDZ1 in
complex with C-peptide (b) and PDZ2 (c). The C-peptide in b is
shown as an explicit atomic model. (d) Comparison of the B/
B
groove conformation in PDZ1 (orange) and PDZ2 of PSD-95
(purple). The two PDZ domains were superimposed on each other
using their respective B
strands. The axis of the B
helix in each PDZ domain is indicated by a solid rod at the
center of the helical cylinder. (e) Surface representation of
the PDZ1 -C-peptide complex. PDZ1 is shown as a surface model,
the backbone of the C-peptide is shown as a white worm, and the
side chains of the last two residues of the C-peptide are shown
as explicit atomic models. The hydrophobic residues of the
surface model are shown in yellow, the positively charged
residues in blue, the negatively charged residues in red and the
rest of amino acids in gray.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2005,
12,
722-728)
copyright 2005.
PDZ
domains determined by NMR spectroscopy. (a -c) Ribbon
diagrams of representative NMR structures of PDZ1 (a), PDZ1 in
complex with C-peptide (b) and PDZ2 (c). The C-peptide in b is
shown as an explicit atomic model. (d) Comparison of the 
B/
B
groove conformation in PDZ1 (orange) and PDZ2 of PSD-95
(purple). The two PDZ domains were superimposed on each other
using their respective