Figure 3.
Figure 3: Comparison of beta-[2]AR
and rhodopsin structures. a, The
[2]AR is superimposed with the homologous structure of
rhodopsin^6. Retinal is shown in purple and the electron density
in the putative ligand-binding site is shown as a green mesh.
Structures were aligned using all seven transmembrane segments.
The right panels represent cross-sections that are rotated
90° around the horizontal axis and viewed from the
extracellular face of the receptor. b, Comparison of the [2]AR
with structures of inactive rhodopsin and light-activated
rhodopsin around the conserved E/DRY sequence in TM3. A
dashed line shows the distance between the homologous arginine
in TM3 and glutamate in TM6. To facilitate comparison of the
E/DRY regions, the structures were aligned by superimposing TM3
only.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2007,
450,
383-387)
copyright 2007.
[2]AR
and rhodopsin structures. a, The 
[2]AR is superimposed with the homologous structure of
rhodopsin^6. Retinal is shown in purple and the electron density
in the putative ligand-binding site is shown as a green mesh.
Structures were aligned using all seven transmembrane segments.
The right panels represent cross-sections that are rotated
90° around the horizontal axis and viewed from the
extracellular face of the receptor. b, Comparison of the