1YCJ
Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate
Summary for 1YCJ
| Entry DOI | 10.2210/pdb1ycj/pdb |
| Related | 1FTJ |
| Descriptor | Ionotropic glutamate receptor 5, SULFATE ION, GLUTAMIC ACID, ... (4 entities in total) |
| Functional Keywords | ionotropic glutamate receptor, kainate receptor, glur5 ligand-binding core, membrane protein |
| Biological source | Rattus norvegicus (Norway rat) More |
| Total number of polymer chains | 2 |
| Total formula weight | 59183.61 |
| Authors | Naur, P.,Vestergaard, B.,Skov, L.K.,Egebjerg, J.,Gajhede, M.,Kastrup, J.S. (deposition date: 2004-12-22, release date: 2005-02-01, Last modification date: 2024-11-13) |
| Primary citation | Naur, P.,Vestergaard, B.,Skov, L.K.,Egebjerg, J.,Gajhede, M.,Kastrup, J.S. Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate Febs Lett., 579:1154-1160, 2005 Cited by PubMed Abstract: The X-ray structure of the ligand-binding core of the kainate receptor GluR5 (GluR5-S1S2) in complex with (S)-glutamate was determined to 1.95 A resolution. The overall GluR5-S1S2 structure comprises two domains and is similar to the related AMPA receptor GluR2-S1S2J. (S)-glutamate binds as in GluR2-S1S2J. Distinct features are observed for Ser741, which stabilizes a highly coordinated network of water molecules and forms an interdomain bridge. The GluR5 complex exhibits a high degree of domain closure (26 degrees) relative to apo GluR2-S1S2J. In addition, GluR5-S1S2 forms a novel dimer interface with a different arrangement of the two protomers compared to GluR2-S1S2J. PubMed: 15710405DOI: 10.1016/j.febslet.2005.01.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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