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1YCJ

Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate

Summary for 1YCJ
Entry DOI10.2210/pdb1ycj/pdb
Related1FTJ
DescriptorIonotropic glutamate receptor 5, SULFATE ION, GLUTAMIC ACID, ... (4 entities in total)
Functional Keywordsionotropic glutamate receptor, kainate receptor, glur5 ligand-binding core, membrane protein
Biological sourceRattus norvegicus (Norway rat)
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Total number of polymer chains2
Total formula weight59183.61
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 citationNaur, 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: 15710405
DOI: 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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