Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors.
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 a...
| Autores principales: | , , , , , , , |
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| Formato: | Journal article |
| Lenguaje: | English |
| Publicado: |
2009
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| _version_ | 1826277148899409920 |
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| author | Clayton, A Siebold, C Gilbert, R Sutton, G Harlos, K McIlhinney, R Jones, E Aricescu, A |
| author_facet | Clayton, A Siebold, C Gilbert, R Sutton, G Harlos, K McIlhinney, R Jones, E Aricescu, A |
| author_sort | Clayton, A |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T23:24:32Z |
| format | Journal article |
| id | oxford-uuid:69e8f918-332d-49f3-afc9-1593b6de2fa7 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:24:32Z |
| publishDate | 2009 |
| record_format | dspace |
| spelling | oxford-uuid:69e8f918-332d-49f3-afc9-1593b6de2fa72022-03-26T18:54:03ZCrystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:69e8f918-332d-49f3-afc9-1593b6de2fa7EnglishSymplectic Elements at Oxford2009Clayton, ASiebold, CGilbert, RSutton, GHarlos, KMcIlhinney, RJones, EAricescu, AIonotropic 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. |
| spellingShingle | Clayton, A Siebold, C Gilbert, R Sutton, G Harlos, K McIlhinney, R Jones, E Aricescu, A Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors. |
| title | Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors. |
| title_full | Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors. |
| title_fullStr | Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors. |
| title_full_unstemmed | Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors. |
| title_short | Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors. |
| title_sort | crystal structure of the glur2 amino terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors |
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