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PDBsum entry 1ycj

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Membrane protein PDB id
1ycj
Contents
Protein chains
251 a.a.
Ligands
SO4 ×7
GLU ×2
Waters ×398

References listed in PDB file
Key reference
Title Crystal structure of the kainate receptor glur5 ligand-Binding core in complex with (s)-Glutamate.
Authors P.Naur, B.Vestergaard, L.K.Skov, J.Egebjerg, M.Gajhede, J.S.Kastrup.
Ref. FEBS Lett, 2005, 579, 1154-1160. [DOI no: 10.1016/j.febslet.2005.01.012]
PubMed id 15710405
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.
Figure 1.
Fig. 1. Ligand-binding cores of the three classes of iGluRs. Cartoon representations of the overall structures of the AMPA receptor GluR2-S1S2J (MolB, pdb code 1FTJ; left figure), the kainate receptor GluR5-S1S2 (MolB; middle figure) and the NMDA receptor NR1-S1S2 (MolA, pdb code 1PB7; right figure). Domain D1 (primarily composed of S1 residues) is colored cyan and D2 (primarily composed of S2 residues) is colored brown. GluR2-S1S2J and GluR5-S1S2 were crystallized in the presence of (S)-glutamate, whereas NR1 was crystallized in complex with (S)-glycine. The ligands are shown in ball-and-stick representation.
Figure 2.
Fig. 2. Comparison of the structures of GluR5-S1S2 and GluR2-S1S2J. (A) Structural alignment of GluR5-S1S2 and GluR2-S1S2J. Boxes correspond to structurally conserved regions. The Gly-Thr linker is shaded grey. (B) Superimposition of the D1 Cα-atoms of the structures of GluR5-S1S2 and GluR2-S1S2J. A Cα-trace of the two structures is shown in stereo, with GluR5-S1S2 coloured in green and GluR2-S1S2J in magenta. Every 10th residue of the GluR5-S1S2 structure is labeled. (S)-glutamate is shown in ball-and-stick.
The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2005, 579, 1154-1160) copyright 2005.
PROCHECK
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