Figure 2.
Figure 2 mGluR binding disrupts the autoinhibitory assemblies of
Tamalin to liberate the Intrinsic ligand. (A) Schematic
representation of the domain structure of Tamalin. Molecules
identified as binding partners and the series of constructs used
in this study are depicted. (B, C) Yeast two-hybrid assays of
hetero- (B) and homotypic (C) interactions of Tamalin. The
independent mating cultures were spotted and then assayed for
-gal
activity. (D) Disruption of the autoinhibitory assembly of
Tamalin by the binding of the mGluR5 C-terminal peptide. We
utilized a pBridge vector (Clontech) instead of pAS2-1, in which
the mGluR5 C-terminus was cloned or not into second multiple
cloning site.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
EMBO J
(2007,
26,
2192-2205)
copyright 2007.
-gal
activity. (D) Disruption of the autoinhibitory assembly of
Tamalin by the binding of the mGluR5 C-terminal peptide. We
utilized a pBridge vector (Clontech) instead of pAS2-1, in which
the mGluR5 C-terminus was cloned or not into second multiple
cloning site.