Figure 1.
Fig. 1. Structure of the Erbin PDZ bound to the
unphosphorylated ErbB2 peptide. A, sequence comparison of
selected class I PDZ domains. Identical residues in four or more
domains are shown as white letters on blue background. Hyphens
represent gaps inserted for optimum alignment. The secondary
structure of the Erbin PDZ is indicated at the top. Residues
forming a short -helix in
PDZs with known structures are enclosed in a red box. B, stereo
view of the Erbin PDZ bound to the peptide EYLGLDVPV. The figure
was made using BOBSCRIPT (30) and POV-Ray (www.povray.org). C,
surface topology of the Erbin PDZ bound to the ErbB2 peptide.
The figure was made using GRASP (31). D, two-dimensional
representation of the interactions between Erbin PDZ residues
(orange) and the peptide (purple). Water molecules (W) are shown
as cyan spheres, hydrogen bonds as dashed lines, and hydrophobic
interactions as arcs with radial spokes. The figure was made
using LIGPLOT (32). E, stereo view of a weighted 2F[obs] F[calc]
electron density map at the P[2] pocket calculated at 1.25
Å and contoured at 2.5 .
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2003,
278,
1399-1402)
copyright 2003.
-helix in
PDZs with known structures are enclosed in a red box. B, stereo
view of the Erbin PDZ bound to the peptide EYLGLDVPV. The figure
was made using BOBSCRIPT (30) and POV-Ray (www.povray.org). C,
surface topology of the Erbin PDZ bound to the ErbB2 peptide.
The figure was made using GRASP (31). D, two-dimensional
representation of the interactions between Erbin PDZ residues
(orange) and the peptide (purple). Water molecules (W) are shown
as cyan spheres, hydrogen bonds as dashed lines, and hydrophobic
interactions as arcs with radial spokes. The figure was made
using LIGPLOT (32). E, stereo view of a weighted 2F[obs] 
F[calc]
electron density map at the P[2] pocket calculated at 1.25
Å and contoured at 2.5 
.