Figure 2.
Figure 2. Structure of the TR D355R
mutant dimer. (A) Cartoon representation of the dimer. The two
TR monomers are shown in green (helixes are numbered) and
yellow. The N- and C-termini of each LBD are labeled. Residues
H412, H413, R355, E324, E326, R338, and sulfate ion at the dimer
interface are shown as stick models and orange sphere,
respectively. The bound hormone is shown as space-filling model
in dark gray. The two boxed regions indicate the crucial polar
interactions at the dimer interface (shown in detail on Panel
B). (B) Network of contacting interfacial residues from two
sites at the dimer interface. Residues are shown as stick
models. Sulfate ion and water are drawn as stick model and
sphere, respectively. Contacts between interacting residues and
ions are indicated. The electron density corresponding to the
sulfate ion (black mesh) in the 2Fo-Fc map is contoured at 2.0
.
(C) Polar dimer interface. The intermolecular residues are in
surface representation for the green monomer, and in stick
representation for the yellow monomer. Shared at interface water
molecules are depicted as cyan dotted spheres. Figures were
prepared with PyMOL from DeLano Scientific
(http://www.pymol.org).
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
75,
111-117)
copyright 2008.
D355R
mutant dimer. (A) Cartoon representation of the dimer. The two
TR monomers are shown in green (helixes are numbered) and
yellow. The N- and C-termini of each LBD are labeled. Residues
H412, H413, R355, E324, E326, R338, and sulfate ion at the dimer
interface are shown as stick models and orange sphere,
respectively. The bound hormone is shown as space-filling model
in dark gray. The two boxed regions indicate the crucial polar
interactions at the dimer interface (shown in detail on Panel
B). (B) Network of contacting interfacial residues from two
sites at the dimer interface. Residues are shown as stick
models. Sulfate ion and water are drawn as stick model and
sphere, respectively. Contacts between interacting residues and
ions are indicated. The electron density corresponding to the
sulfate ion (black mesh) in the 2Fo-Fc map is contoured at 2.0
.
(C) Polar dimer interface. The intermolecular residues are in
surface representation for the green monomer, and in stick
representation for the yellow monomer. Shared at interface water
molecules are depicted as cyan dotted spheres. Figures were
prepared with PyMOL from DeLano Scientific
(http://www.pymol.org).