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  Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluRD

Kuusinen, A., Abele, R., Madden, D. R., & Keinänen, K. (1999). Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluRD. The Journal of Biological Chemistry, 274(41), 28937-28943. doi:10.1074/jbc.274.41.28937.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-A692-2 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-A693-F
Genre: Journal Article
Alternative Title : Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluRD

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JBiolChem_274_1999_28937.pdf (Any fulltext), 255KB
 
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 Creators:
Kuusinen, Arja, Author
Abele, Rupert1, Author           
Madden, Dean R.1, Author           
Keinänen, Kari, Author
Affiliations:
1Max Planck Research Group Ion Channel Structure (Dean R. Madden), Max Planck Institute for Medical Research, Max Planck Society, ou_1497725              

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 Abstract: 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 alpha -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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Language(s): eng - English
 Dates: 1999-07-201999-03-221999-10-08
 Publication Status: Issued
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666558
DOI: 10.1074/jbc.274.41.28937
URI: http://www.ncbi.nlm.nih.gov/pubmed/10506139
URI: http://www.jbc.org/cgi/content/full/274/41/28937
URI: http://www.jbc.org/cgi/reprint/274/41/28937
Other: 4441
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 274 (41) Sequence Number: - Start / End Page: 28937 - 28943 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1