3FAS

X-ray structure of iGluR4 flip ligand-binding core (S1S2) in complex with (S)-glutamate at 1.40A resolution

Summary for 3FAS

• Entry DOI: 10.2210/pdb3fas/pdb
• Related: 1ftj 1ftm 2uxa
• Descriptor: Glutamate receptor 4, GLUTAMIC ACID, SULFATE ION, ... (5 entities in total)
• Functional Keywords: ionotropic glutamate receptors, iglur4, flip, ligand-binding core, agonist complex, membrane protein
• Biological source: Rattus norvegicus (RAT); More
• Cellular location: Cell membrane; Multi-pass membrane protein: P19493
• Total number of polymer chains: 2
• Total formula weight: 59932.69

Authors

Kasper, C.,Frydenvang, K.,Naur, P.,Gajhede, M.,Kastrup, J.S. (deposition date: 2008-11-18, release date: 2008-12-09, Last modification date: 2024-11-13)

Primary citation

Kasper, C.,Frydenvang, K.,Naur, P.,Gajhede, M.,Pickering, D.S.,Kastrup, J.S.
Molecular mechanism of agonist recognition by the ligand-binding core of the ionotropic glutamate receptor 4
Febs Lett., 582:4089-4094, 2008

PubMed Abstract: The alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) class of ionotropic glutamate receptors comprises four different subunits: iGluR1/iGluR2 and iGluR3/iGluR4 forming two subgroups. Three-dimensional structures have been reported only of the ligand-binding core of iGluR2. Here, we present two X-ray structures of a soluble construct of the R/G unedited flip splice variant of the ligand-binding core of iGluR4 (iGluR4(i)(R)-S1S2) in complex with glutamate or AMPA. Subtle, but important differences are found in the ligand-binding cavity between the two AMPA receptor subgroups at position 724 (Tyr in iGluR1/iGluR2 and Phe in iGluR3/iGluR4), which in iGluR4 may lead to displacement of a water molecule and hence points to the possibility to make subgroup specific ligands.

PubMed: 19022251
DOI: 10.1016/j.febslet.2008.11.005

Experimental method

X-RAY DIFFRACTION (1.4 Å)