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PDBsum entry 2i3w
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Membrane protein
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PDB id
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2i3w
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References listed in PDB file
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Key reference
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Title
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Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor.
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Authors
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N.Armstrong,
J.Jasti,
M.Beich-Frandsen,
E.Gouaux.
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Ref.
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Cell, 2006,
127,
85-97.
[DOI no: ]
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PubMed id
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Abstract
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The canonical conformational states occupied by most ligand-gated ion channels,
and many cell-surface receptors, are the resting, activated, and desensitized
states. While the resting and activated states of multiple receptors are well
characterized, elaboration of the structural properties of the desensitized
state, a state that is by definition inactive, has proven difficult. Here we use
electrical, chemical, and crystallographic experiments on the AMPA-sensitive
GluR2 receptor, defining the conformational rearrangements of the agonist
binding cores that occur upon desensitization of this ligand-gated ion channel.
These studies demonstrate that desensitization involves the rupture of an
extensive interface between domain 1 of 2-fold related glutamate-binding core
subunits, compensating for the ca. 21 degrees of domain closure induced by
glutamate binding. The rupture of the domain 1 interface allows the ion channel
to close and thereby provides a simple explanation to the long-standing question
of how agonist binding is decoupled from ion channel gating upon receptor
desensitization.
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Figure 1.
Figure 1. MTSES Modification of E486C in Closed, Open, and
Desensitized States
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Figure 7.
Figure 7. Mechanism of Activation and Desensitization
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2006,
127,
85-97)
copyright 2006.
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Secondary reference #1
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Title
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Probing the ligand binding domain of the glur2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct.
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Authors
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G.Q.Chen,
Y.Sun,
R.Jin,
E.Gouaux.
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Ref.
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Protein Sci, 1998,
7,
2623-2630.
[DOI no: ]
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PubMed id
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