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Figure 2.
Fig. 2. Structure of hRAR  LBD bound
to the inactive BMS270395 and its comparison with the BMS270394
complex (stereo representations) (A). The BMS270395 complex with
the initial refinement-unbiased  [A]-weighted
F[obs]  F[calc]
map at 1.67 Å resolution contoured at 3.2 and
colored in violet. The map clearly indicates two possible
positions for the fluorine atom, corresponding to two different
ligand conformations. The up and down orientations of the
fluorine atom have occupancies of 40/60%, respectively (colored
in green and red, pointing to Ile-275 and Ala-234, respectively)
(B). Superposition of the hRAR LBD
complexes of both enantiomers as obtained by a least-squares
fit. The position of the hydroxyl group oxygen is strictly
conserved to maintain the hydrogen bond to Met-272; BMS270395
therefore adopts a conformation different from that observed for
BMS270394 (C). Detailed view of the part of the ligand pocket
where the ligand exhibits unfavorable contacts. The color code
for distances is that of Fig. 1. The fluorine atom exhibits
close contacts for both the up and down orientation, whereas the
salt bridge between the carboxylate group and Arg-278 is weaker
compared with the BMS270394 complex.
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