| Title : Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors - Clayton_2009_J.Mol.Biol_392_1125 |
| Author(s) : Clayton A , Siebold C , Gilbert RJ , Sutton GC , Harlos K , McIlhinney RA , Jones EY , Aricescu AR |
| Ref : Journal of Molecular Biology , 392 :1125 , 2009 |
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Abstract :
Ionotropic glutamate receptors are functionally diverse but have a common architecture, including the 400-residue amino-terminal domain (ATD). We report a 1.8-A resolution crystal structure of human GluR2-ATD. This dimeric structure provides a mechanism for how the ATDs can drive receptor assembly and subtype-restricted composition. Lattice contacts in a 4.1-A resolution crystal form reveal a tetrameric (dimer-dimer) arrangement consistent with previous cellular and cryo-electron microscopic data for full-length AMPA receptors. |
| PubMedSearch : Clayton_2009_J.Mol.Biol_392_1125 |
| PubMedID: 19651138 |
Clayton A, Siebold C, Gilbert RJ, Sutton GC, Harlos K, McIlhinney RA, Jones EY, Aricescu AR (2009)
Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors
Journal of Molecular Biology
392 :1125
Clayton A, Siebold C, Gilbert RJ, Sutton GC, Harlos K, McIlhinney RA, Jones EY, Aricescu AR (2009)
Journal of Molecular Biology
392 :1125