PDBsum entry 1ycj

Membrane protein

PDB id: 1ycj

Contents

Protein chains

251 a.a. *

Ligands

SO4 ×7

GLU ×2

Waters ×398

* Residue conservation analysis

PDB id:

1ycj

Name:

Membrane protein

Title:

Crystal structure of the kainate receptor glur5 ligand-binding core in complex with (s)-glutamate

Structure:

Ionotropic glutamate receptor 5. Chain: a, b. Fragment: glur5 ligand-binding core. Synonym: glutamate receptor, ionotropic kainate 1. Glur-5. Glur5. Glutamate receptor subunit 5-2. Engineered: yes

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: grik1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Trimer (from PQS)

Resolution:

1.95Å R-factor: 0.203 R-free: 0.269

Authors:

P.Naur,B.Vestergaard,L.K.Skov,J.Egebjerg,M.Gajhede,J.S.Kastrup

Key ref:

P.Naur et al. (2005). Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate. FEBS Lett, 579, 1154-1160. PubMed id: 15710405 DOI: 10.1016/j.febslet.2005.01.012

Date:

22-Dec-04 Release date: 01-Feb-05

Protein chains

P22756  (GRIK1_RAT) -  Glutamate receptor ionotropic, kainate 1 from Rattus norvegicus

Seq: 949 a.a.

Struc: 251 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1016/j.febslet.2005.01.012

FEBS Lett 579:1154-1160 (2005)

PubMed id: 15710405

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

P.Naur, B.Vestergaard, L.K.Skov, J.Egebjerg, M.Gajhede, J.S.Kastrup.

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.

Selected figure(s)

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.

Figures were selected by an automated process.