Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate |
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| Authors: | Naur Peter Vestergaard Bente Skov Lars K Egebjerg Jan Gajhede Michael Kastrup Jette Sandholm |
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| Affiliation: | Biostructural Research, Department of Medicinal Chemistry, Danish University of Pharmaceutical Sciences, Universitetsparken 2, DK-2100 Copenhagen, Denmark. |
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| 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. |
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| Keywords: | 4-AHCP, 2-amino-3-(3-hydroxy-7,8-dihydro-6H-cyclohepta[d]-4-isoxazolyl)propionate AMPA, 2-amino-3-(3-hydroxy-5-methyl-4-isoxazolyl)propionate ATPA, 2-amino-3-(5-tert-butyl-3-hydroxy-4-isoxazolyl)propionate E. coli, Escherichia coli EDTA, ethylenediaminetetraacetate GluR2-S1S2J, ligand-binding core construct of GluR2 GluR5-S1S2, ligand-binding core construct of GluR5 HEPES, N-2-hydroxyethylpiperazine-N′-2-ethanesulfonate iGluR, ionotropic glutamate receptor IPTG, isopropyl-β-d-thiogalactopyranoside M1-M3, three transmembrane spanning regions NMDA, N-methyl-d-aspartate NR1-S1S2, ligand-binding core construct of NR1 r.m.s.d., root mean square deviation PCR, polymerase chain reaction PEG, polyethylene glycol vdW, van der Waals |
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