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J Biol Chem, Vol. 274, Issue 41, 28937-28943, October 8, 1999

Oligomerization and Ligand-binding Properties of the Ectodomain of the -Amino-3-hydroxy-5-methyl-4-isoxazole Propionic Acid Receptor Subunit GluRD

Arja Kuusinen^§, Rupert Abele^¶, Dean R. Madden^¶, and Kari Keinänen^§

From the  Viikki Biocenter, Department of Biosciences, Division of Biochemistry, and Institute of Biotechnology, P. O. Box 56, FIN-00014 University of Helsinki, Finland, ^§ VTT Biotechnology and Food Research, P. O. Box 1500, FIN-02044 VTT, Espoo, Finland, and the ^¶ Ion Channel Structure Research Group, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany

The extracellular part of ionotropic glutamate receptor (iGluR) subunits can be divided into a conserved two-lobed ligand-binding domain ("S1S2") and an N-terminal ~400-residue segment of unknown function ("X domain") which shows high sequence variation among subunits. To investigate the structure and properties of the N-terminal domain, we have now produced affinity-tagged recombinant fragments which represent the X domain of the GluRD subunit of -amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective glutamate receptors either alone or covalently linked to the ligand-binding domain ("XS1S2"). These fragments were expressed in insect cells as secreted soluble proteins and were recognized by a conformation-specific anti-GluRD monoclonal antibody. A hydrodynamic analysis of the purified fragments revealed them to be dimers, in contrast to the S1S2 ligand-binding domain which is monomeric. The X domain did not bind radiolabeled AMPA or glutamate nor did its presence affect the ligand binding properties of the S1S2 domain. Our findings demonstrate that the N-terminal domain of AMPA receptor can be expressed as a soluble polypeptide and suggest that subunit interactions in iGluR may involve the extracellular domains.

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