Figure 1.
Figure 1. Solution structure of the p55 PDZ domain. (A) Stereo
view of the 20 final structures of the p55 PDZ domain (residues
69-153). The superposition of the backbone atoms (N, C ,
and C )
is shown. (B) Ribbon diagram of the energy-minimized average
structure of the p55 PDZ domain. The -helices
are shown in red, and the -strands
are cyan. The secondary structure elements are labeled according
to the scheme used in the crystal structure of PSD95 PDZ3.[8]
(C) Superposition of the PDZ domain of p55 (blue) with those of
PSD95-PDZ3^8 (red), hCASK^10 (green), InaD[27] (yellow),
GRIP1-PDZ6[28] (cyan), and AF-6[29] (purple). (D) Space-filling
model of the groove between strand B
and helix B
of the p55 PDZ domain. Basic, acidic and hydrophobic amino acids
are shown in blue, red and yellow, respectively. (E)
Identification of the GPC-binding site on the p55 PDZ domain by
the chemical shift perturbation experiment. The residues (Gly83,
Thr85, Leu86, Leu88, Val125, Ser129, Val130, Gln134, Met137, and
Glu139) showing large chemical shift changes caused by the
addition of a 10-fold molar excess of peptide are labeled and
colored purple. With the exception of Val125, all of these
residues reside on one side of the protein surface.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2006,
64,
804-807)
copyright 2006.
,
and C 
)
is shown. (B) Ribbon diagram of the energy-minimized average
structure of the p55 PDZ domain. The 
-strands
are cyan. The secondary structure elements are labeled according
to the scheme used in the crystal structure of PSD95 PDZ3.[8]
(C) Superposition of the PDZ domain of p55 (blue) with those of
PSD95-PDZ3^8 (red), hCASK^10 (green), InaD[27] (yellow),
GRIP1-PDZ6[28] (cyan), and AF-6[29] (purple). (D) Space-filling
model of the groove between strand