5IKB

Crystal structure of the kainate receptor GluK4 ligand binding domain in complex with kainate

Summary for 5IKB

• Entry DOI: 10.2210/pdb5ikb/pdb
• Descriptor: Glutamate receptor ionotropic, kainate 4,Glutamate receptor ionotropic, kainate 4, 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: high-affinity kainate receptor, membrane protein, ligand binding domain, ion channel
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 1
• Total formula weight: 29568.63

Authors

Kristensen, O.,Kristensen, L.B.,Frydenvang, K.,Kastrup, J.S. (deposition date: 2016-03-03, release date: 2016-08-24, Last modification date: 2024-01-10)

Primary citation

Kristensen, O.,Kristensen, L.B.,Mollerud, S.,Frydenvang, K.,Pickering, D.S.,Kastrup, J.S.
The Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate.
Structure, 24:1582-1589, 2016

PubMed Abstract: Ionotropic glutamate receptors play a key role in fast neurotransmission in the CNS and have been linked to several neurological diseases and disorders. One subfamily is the kainate receptors, which are grouped into low-affinity (GluK1-3) and high-affinity (GluK4-5) receptors based on their affinity for kainate. Although structures of the ligand-binding domain (LBD) of all low-affinity kainate receptors have been reported, no structures of the high-affinity receptor subunits are available. Here, we present the X-ray structure of GluK4-LBD with kainate at 2.05 Å resolution, together with thermofluor and radiolabel binding affinity data. Whereas binding-site residues in GluK4 are most similar to the AMPA receptor subfamily, the domain closure and D1-D2 interlobe contacts induced by kainate are similar to the low-affinity kainate receptor GluK1. These observations provide a likely explanation for the high binding affinity of kainate at GluK4-LBD.

PubMed: 27524200
DOI: 10.1016/j.str.2016.06.019

Experimental method

X-RAY DIFFRACTION (2.05 Å)