Biomedical Engineering Reference
In-Depth Information
N
Cl
*
R
NH
H 2 NO 2 S
S
NH
OO
S
OO
CTZ ( 15.80 )
15.116
*
*
*
NH
HN
NH
S
OO
S
S
O
O
O
O
15.117
15.118
FIGURE 15.23 Structure of CTZ ( 15.80 ), and other positive allosteric modulators at AMPA receptors
including the symmetric dimeric analog 15.118 .
(B)
(A)
(C)
FIGURE 15.24 (A) X-ray structure of the upper part of the extracellular amino terminal domain of the
GluR2 receptor in complex with CTZ ( 15.80 ) (white carbon atoms). (B) Illustration of the binding of dimer
15.118 (cyan carbon atoms) compared to the binding of CTZ (white carbon atoms) in the calculated cavity
formed by the binding pocket surface (side-view). (C) Close-up-view of the x-ray structure of the GluR2 recep-
tor in complex with dimer 15.118 (brown carbon atoms) compared to CTZ (white carbon atoms).
15.10 CONCLUDING REMARKS
The cloning of the GABA and Glu receptor subtypes and their pharmacological characterization has
been of great importance to the development of the i eld. For the Glu area a large number of crys-
tal structure determinations has afforded valuable information about these receptors, their mecha-
nism of action and the 3D information about binding sites is used extensively for the design and
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