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  First images of a glutamate receptor ion channel: oligomeric state and molecular dimensions of GluRB homomers

Safferling, M., Tichelaar, W., Kümmerle, G., Jouppila, A., Kuusinen, A., Keinänen, K., et al. (2001). First images of a glutamate receptor ion channel: oligomeric state and molecular dimensions of GluRB homomers. Biochemistry, 40(46), 13948-13953. doi:10.1021/bi011143g.

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Alternative Title : First images of a glutamate receptor ion channel: oligomeric state and molecular dimensions of GluRB homomers

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 Creators:
Safferling, Markus1, Author              
Tichelaar, Willem2, Author              
Kümmerle, Günther1, Author              
Jouppila, Annukka, Author
Kuusinen, Arja, Author
Keinänen, Kari, Author
Madden, Dean R.1, Author              
Affiliations:
1Max Planck Research Group Ion Channel Structure (Dean R. Madden), Max Planck Institute for Medical Research, Max Planck Society, ou_1497725              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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 Abstract: We have expressed, purified, and characterized glutamate receptor ion channels (GluR) assembled as homomers of the subunit GluRB. For the first time, single-milligram quantities of biochemically homogeneous GluR have been obtained. The protein exhibits the expected pharmacological profile and a high specific activity for ligand binding. Density-gradient centrifugation reveals a uniform oligomeric assembly and a molecular mass suggesting that the channel is a tetramer. On the basis of electron microscopic images, the receptor appears to form an elongated structure that is visualized in several orientations. The molecular dimensions of the molecule are approximately 11 x 14 x 17 nm, and solvent-accessible features can be seen; these may contribute to formation of the ion-conducting pathway of the channel. The channel dimensions are consistent with an overall 2-fold symmetric assembly, suggesting that the tetrameric receptor may be a dimer of dimers.

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Language(s): eng - English
 Dates: 2001-06-042001-09-052001-11-20
 Publication Status: Published in print
 Pages: 6
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 Table of Contents: -
 Rev. Type: Peer
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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 40 (46) Sequence Number: - Start / End Page: 13948 - 13953 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103