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  Ligand-protein interactions in the glutamate receptor

Jayaraman, V., Keesey, R., & Madden, D. R. (2000). Ligand-protein interactions in the glutamate receptor. Biochemistry, 39, 8693-8697. doi:10.1021/bi000892f.

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Genre: Journal Article
Alternative Title : Ligand-protein interactions in the glutamate receptor

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Biochem_39_2000_8693.pdf (Any fulltext), 216KB
 
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 Creators:
Jayaraman, Vasanthi, Author
Keesey, Robert, Author
Madden, Dean R.1, Author           
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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: Fourier transform infrared spectroscopy was used to investigate ligand-protein interactions in the ligand-binding domain of the GluR4 glutamate receptor subunit. Glutamate binding induces more extensive secondary structural changes in the ligand-binding domain than does kainate binding. Glutamate also alters the hydrogen bonding strength of the single free cysteine side chain in the domain, while kainate does not. On the other hand, the interaction of a binding site arginine residue with kainate appears to be stronger than that with glutamate. These results identify chemical and structural differences that may explain the different functional characteristics of the two agonists acting on ionotropic glutamate receptors. In doing so, they complement and extend recent crystallographic structures of the ligand-binding domain.

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Language(s): eng - English
 Dates: 2000-04-192000-07-072000-08-01
 Publication Status: Issued
 Pages: 5
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 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: 39 Sequence Number: - Start / End Page: 8693 - 8697 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103