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Chimeric receptor subunits of the AMPA receptor subunit GluR2 and the kainate receptor subunit GluR6 were constructed and stably expressed in baby hamster kidney cells. By using Ca2+ imaging and radioligand binding, we demonstrated that substitution of a specific domain showing homology to a bacterial leucine-isoleucine-valine binding protein (LIVBP) had no effect on the affinities of the tested agonists, but decreased the affinities of the antagonists CNQX, DNQX, and NBQX. On the other hand, when the first of two domains showing homology to a bacterial glutamine binding protein (QBP) in GluR2 was substituted with the corresponding region from GluR6, the affinity of AMPA decreased sevenfold and the affinity of kainate increased fourfold, indicating the importance of this domain in binding of these agonists. In contrast to this, the affinities of quisqualate and domoate, two other agonists, were unchanged, indicating that a region located C-terminal to the QBP domain is also involved in agonist binding.
C K Tygesen, and
M Jørgensen, and
P H Andersen
June 1998,
Brain research,
C K Tygesen, and
M Jørgensen, and
P H Andersen
February 2009,
Annals of neurology,
C K Tygesen, and
M Jørgensen, and
P H Andersen
December 1995,
Neuroscience research,
C K Tygesen, and
M Jørgensen, and
P H Andersen
January 2003,
Doklady. Biochemistry and biophysics,
C K Tygesen, and
M Jørgensen, and
P H Andersen
August 2009,
Proteins,
C K Tygesen, and
M Jørgensen, and
P H Andersen
September 2017,
ACS chemical neuroscience,
C K Tygesen, and
M Jørgensen, and
P H Andersen
June 2004,
The Journal of biological chemistry,
C K Tygesen, and
M Jørgensen, and
P H Andersen
February 1984,
Neuroscience letters,
C K Tygesen, and
M Jørgensen, and
P H Andersen
January 2003,
Brain research. Molecular brain research,
C K Tygesen, and
M Jørgensen, and
P H Andersen
December 2002,
Bioscience, biotechnology, and biochemistry,
