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Figure 2.
Figure 2. Schematic Representation of the Ligand binding
Pocket of the ERR3 LBD(A) In the crystal structure, the
positions of all shown side chains are well defined, with the
exception of that of E275, which exhibits high temperature
factors. All atoms are colored according to the following code:
carbon, gray; oxygen, red; nitrogen, blue; sulfur, yellow.(B)
View as in (A) with E2 docked into the empty ligand binding
cavity of ERR3. The position of E2 results from the
superposition of the ERR3 LBD and the ERα LBD/E2 complex.
Steric interference with the D-ring of E2 is mainly due to the
presence of F435 (L525 in hERα) and L345 (I424 in hERα) in
ERR3.(C) Schematic comparison of amino acid residues that form
the ligand binding pocket in hERR3 with the corresponding
residues of hERR2, hERR1, and hERα. Residues that are conserved
among all four receptors are depicted in yellow, and those
conserved among the ERR isotypes are colored in blue. Amino
acids of hERα that according to our modeling studies allow the
binding of E2 to ERs but not to ERRs are highlighted in red.
Important isotype-specific amino acid differences are colored in
green.
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