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] |
Constructs are labeled as described by the authors. All genes are from Rattus novergicus.
AC pair distances are measured between the Cα atoms of R660 for GluA2, K664 for GluK2.
BD pair distances are measured between the Cα atoms of Q756 for GluA2, E757 for GluK2.
Toxin: a Conus striatus cone snail toxin, con-ikot-ikot [6].
References:
Durr, K.L. et al. (2014) Structure and dynamics of AMPA receptor GluA2 in resting, pre-open, and desensitized states. Cell 158, 778-792.
Sobolevsky, A.I. et al. (2009) X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462, 745-756.
Yelshanskaya, M.V. et al. (2014) Structure of an agonist-bound ionotropic glutamate receptor. Science 345, 1070-1074.
Meyerson, J.R. et al. (2014) Structural mechanism of glutamate receptor activation and desensitization. Nature 514, 328-334.
Chen, L. et al. (2014) X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism. Science 345, 1021-1026.
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.