Figure 1.
Figure 1. Solution structure of the 4.1R -lobe
domain. (A) Stereo view of the 20 final structures of the 4.1R
-lobe
domain. The superposition of the backbone atoms (N, C ,
and C )
is shown. (B) Ribbon diagram of the final lowest energy
structure of the 4.1R -lobe
domain. The secondary structure elements are labeled. (C)
Superposition of the NMR structure determined in this study
(green) with the crystal structure of the -lobe
domain (blue) in the 4.1R FERM domain (PDB code 1GG3).[9] The
N-lobe domain is shown in yellow, the -lobe
domain in blue, and the C-lobe domain in red. (D) Identification
of the GPC-binding site on the 4.1R -lobe
domain. The orientation of the left image in this panel is the
same as that in panel B. The right image in this panel is
related to that in the left image by a 180° rotation along
the vertical axis. The residues showing large chemical shift
changes ( z0.1
ppm), caused by the addition of a 10-fold molar excess of GPC,
(82-128) are colored red. Almost all of these residues reside on
one side of the protein surface. The ELEE motif is colored
orange.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2009,
76,
255-260)
copyright 2009.
-lobe
domain. (A) Stereo view of the 20 final structures of the 4.1R
)
is shown. (B) Ribbon diagram of the final lowest energy
structure of the 4.1R 
z0.1
ppm), caused by the addition of a 10-fold molar excess of GPC,
(82-128) are colored red. Almost all of these residues reside on
one side of the protein surface. The ELEE motif is colored
orange.