Motion in Glur2 ligand-binding core [glur2]

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Classification [D-h-2]

Structures 1FTO from rat; open 1FTM closed

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

References 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 function ion channel activity, glutamate-gated ion channel activity, receptor activity, potassium channel activity, ionotropic glutamate receptor activity, transporter activity Cellular component membrane Biological process potassium ion transport, transport, ion transport

Morphs

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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_ yale.edu