Figures and Tables

From the following article:

Mechanism of glutamate receptor desensitization

Yu Sun, Rich Olson, Michelle Horning, Neali Armstrong, Mark Mayer and Eric Gouaux

Nature 417, 245-253(16 May 2002)

doi:10.1038/417245a

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Figure 1

The L483Y mutation and CTZ promote dimerization and block desensitization.

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Figure 2

The L483Y mutation and CTZ stabilize the GluR2 S1S2J dimer.

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Figure 3

Disruption of the Tyr 483 binding site at the dimer interface increases the extent of receptor desensitization and shifts the S1S2J monomer–dimer equilibrium towards monomer.

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Figure 4

Introduction of aspartate at position 754 accelerates desensitization and reveals a new, 'lateral' mode by which the ligand-binding cores can interact.

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Figure 5

Agonist-induced conformational changes in the dimer and gating model.

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Table 1

Dimer dissociation measurements and functional analysis of desensitization

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Table 2

Crystallographic refinement statistics

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