2QS2

Crystal structure of the GluR5 ligand binding core dimer in complex with UBP318 at 1.80 Angstroms resolution

Summary for 2QS2

• Entry DOI: 10.2210/pdb2qs2/pdb
• Related: 1TXF 2F34 2F35 2F36 2QS1 2QS3 2QS4
• Descriptor: Glutamate receptor, ionotropic kainate 1, CHLORIDE ION, PENTAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: membrane protein, cell junction, glycoprotein, ion transport, ionic channel, phosphorylation, postsynaptic cell membrane, receptor, rna editing, synapse, transmembrane, transport
• Biological source: Rattus norvegicus (rat); More
• Cellular location: Cell membrane; Multi-pass membrane protein: P22756
• Total number of polymer chains: 2
• Total formula weight: 59806.96

Authors

Alushin, G.M.,Jane, D.E.,Mayer, M.L. (deposition date: 2007-07-30, release date: 2008-08-05, Last modification date: 2023-08-30)

Primary citation

Alushin, G.M.,Jane, D.,Mayer, M.L.
Binding site and ligand flexibility revealed by high resolution crystal structures of GluK1 competitive antagonists.
Neuropharmacology, 60:126-134, 2011

PubMed Abstract: The availability of crystal structures for the ligand binding domains of ionotropic glutamate receptors, combined with their key role in synaptic function in the normal and diseased brain, offers a unique selection of targets for pharmaceutical research compared to other drug targets for which the atomic structure of the ligand binding site is not known. Currently only a few antagonist structures have been solved, and these reveal ligand specific conformational changes that hinder rational drug design. Here we report high resolution crystal structures for three kainate receptor GluK1 antagonist complexes which reveal new and unexpected modes of binding, highlighting the continued need for experimentally determined receptor-ligand complexes.

PubMed: 20558186
DOI: 10.1016/j.neuropharm.2010.06.002

Experimental method

X-RAY DIFFRACTION (1.8 Å)