Motion in Glur2 ligand-binding core [glur2]

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Classification [D-h-2]

1FTO from rat; open
1FTM closed

This motion is essentially identical to the glutamine binding protein, whose structures have been solved in E. coli.

G Q Chen, Y Sun, R Jin, E Gouaux (1998). Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct. Protein Sci, 7:2623-30 [Medline info for 9865957]
N Armstrong, E Gouaux (2000). Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron, 28:165-81 [Medline info for 11086992]

GO terms associated with structures
Molecular functionglutamate-gated ion channel activity, receptor activity, potassium channel activity, ionotropic glutamate receptor activity, transporter activity, ion channel activity
Cellular componentmembrane
Biological processpotassium ion transport, transport, ion transport


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Best representative
Morph Morph name Structure #1 Structure #2 Residues
Glur2 (with and without Ampa) 1fto [ B ] 1ftm [ B ] 263

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
048243-536 glur2 1fto [ A ] 1ftm [ A ] 263
990832-26206 Glur2 (with and without glutamine) 1ftm [ A ] 1ftj [ A ] 263
962947-27237 GluR2 Open-Apo upload [ A ] upload [ A ] 257
964237-32170 GluR2_Open-Apo upload [ A ] upload [ A ] 257

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_