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. Author manuscript; available in PMC: 2016 Jun 1.
Published in final edited form as: Trends Biochem Sci. 2015 May 1;40(6):328–337. doi: 10.1016/j.tibs.2015.04.002

Table 1.

Structures of intact non-NMDA ionotropic glutamate receptors

PDB ID Constructsa Agonists/
antagonists
Allosteric
modulator
Technique Resolution
(Å)
AC pair
distancesb
(Å)
BD pair
distancesc
(Å)
Reference
Apo form 4U2P GluA25M - - X-RAY 3.24 32.0 21.9 [1]
Antagonist
–bound
form
3KG2 GluA2cryst ZK-200775 - X-RAY 3.60 23.9 24.1 [2]
4U4G GluA2* ZK-200775 - X-RAY 4.49 25.3 24.5 [3]
4UQJ GluA2em ZK-200775 - Cryo-EM ~10.0 27.2 28.0 [4]
Agonist-
bound
form with
allosteric
modulators
4U1W GluA25M Kainate (R,R)-2b X-RAY 3.25 39.8 25.7 [1]
4U1X GluA210M Kainate (R,R)-2b X-RAY 3.30 38.5 25.4 [1]
4U1Y GluA210MDel Fluorowilliardiine (R,R)-2b X-RAY 3.90 39.9 25.8 [1]
4U5D GluA2cryst1 Kainate (R,R)-2b
+toxind
X-RAY 3.58 28.1 21.7 [5]
4U5F GluA2cryst2 Kainate (R,R)-2b
+toxind
X-RAY 3.70 27.8 21.7 [5]
4U5C GluA2cryst1 Fluorowilliardiine (R,R)-2b
+toxind
X-RAY 3.69 27.4 22.0 [5]
4U5E GluA2cryst1
T625G
Kainate (R,R)-2b
+toxind
X-RAY 3.51 27.9 21.8 [5]
4U5B GluA2cryst1
A622T
Kainate (R,R)-2b
+toxind
X-RAY 3.50 27.9 21.8 [5]
4UQ6 GluA2em Glutamate LY451646 Cryo-EM ~12.0 40.2 30.5 [4]
4UQK GluA2em Quisqualate LY451646 Cryo-EM ~16.0 41.6 33.0 [4]
Agonist-
bound
form
4U4F GluA2* (S)-5
-nitrowillardiine
(NOW)
- X-RAY 4.79 29.3 22.3 [3]
4U2Q GluA25M Kainate - X-RAY 3.53 39.3 25.1 [1]
- GluA25M Fluorowilliardiine - X-RAY 7.94 33.9 55.8 [1]
4UQQ GluK2em 2S,4R-4-
methylglutamate
- Cryo-EM ~7.6 32.8 98.5 [4]
a

Constructs are labeled as described by the authors. All genes are from Rattus novergicus.

b

AC pair distances are measured between the Cα atoms of R660 for GluA2, K664 for GluK2.

c

BD pair distances are measured between the Cα atoms of Q756 for GluA2, E757 for GluK2.

d

Toxin: a Conus striatus cone snail toxin, con-ikot-ikot [6].

References:

1

Durr, K.L. et al. (2014) Structure and dynamics of AMPA receptor GluA2 in resting, pre-open, and desensitized states. Cell 158, 778-792.

2

Sobolevsky, A.I. et al. (2009) X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462, 745-756.

3

Yelshanskaya, M.V. et al. (2014) Structure of an agonist-bound ionotropic glutamate receptor. Science 345, 1070-1074.

4

Meyerson, J.R. et al. (2014) Structural mechanism of glutamate receptor activation and desensitization. Nature 514, 328-334.

5

Chen, L. et al. (2014) X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism. Science 345, 1021-1026.

6

Walker, C.S. et al. (2009) A novel Conus snail polypeptide causes excitotoxicity by blocking desensitization of AMPA receptors. Current biology : CB 19, 900-908.

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