Glutamate receptors as seen by light: spectroscopic studies of structure-function relationships

Detalhes bibliográficos
Autor(a) principal: Mankiewicz,K.A.
Data de Publicação: 2007
Outros Autores: Jayaraman,V.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Journal of Medical and Biological Research
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2007001100001
Resumo: Ionotropic glutamate receptors are major excitatory receptors in the central nervous system and also have a far reaching influence in other areas of the body. Their modular nature has allowed for the isolation of the ligand-binding domain and for subsequent structural studies using a variety of spectroscopic techniques. This review will discuss the role of specific ligand:protein interactions in mediating activation in the a-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid subtype of glutamate receptors as established by various spectroscopic investigations of the GluR2 and GluR4 subunits of this receptor. Specifically, this review will provide an introduction to the insight gained from X-ray crystallography and nuclear magnetic resonance investigations and then go on to focus on studies utilizing vibrational spectroscopy and fluorescence resonance energy transfer to study the behavior of the isolated ligand-binding domain in solution and discuss the importance of specific ligand:protein interactions in the mechanism of receptor activation.
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spelling Glutamate receptors as seen by light: spectroscopic studies of structure-function relationshipsVibrational spectroscopyFluorescence resonance energy transfera-Amino-3-hydroxy- 5-methyl-4- isoxazolepropionic acid receptorsAgonist activationLigand bindingIonotropic glutamate receptors are major excitatory receptors in the central nervous system and also have a far reaching influence in other areas of the body. Their modular nature has allowed for the isolation of the ligand-binding domain and for subsequent structural studies using a variety of spectroscopic techniques. This review will discuss the role of specific ligand:protein interactions in mediating activation in the a-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid subtype of glutamate receptors as established by various spectroscopic investigations of the GluR2 and GluR4 subunits of this receptor. Specifically, this review will provide an introduction to the insight gained from X-ray crystallography and nuclear magnetic resonance investigations and then go on to focus on studies utilizing vibrational spectroscopy and fluorescence resonance energy transfer to study the behavior of the isolated ligand-binding domain in solution and discuss the importance of specific ligand:protein interactions in the mechanism of receptor activation.Associação Brasileira de Divulgação Científica2007-11-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2007001100001Brazilian Journal of Medical and Biological Research v.40 n.11 2007reponame:Brazilian Journal of Medical and Biological Researchinstname:Associação Brasileira de Divulgação Científica (ABDC)instacron:ABDC10.1590/S0100-879X2007001100001info:eu-repo/semantics/openAccessMankiewicz,K.A.Jayaraman,V.eng2007-11-09T00:00:00Zoai:scielo:S0100-879X2007001100001Revistahttps://www.bjournal.org/https://old.scielo.br/oai/scielo-oai.phpbjournal@terra.com.br||bjournal@terra.com.br1414-431X0100-879Xopendoar:2007-11-09T00:00Brazilian Journal of Medical and Biological Research - Associação Brasileira de Divulgação Científica (ABDC)false
dc.title.none.fl_str_mv Glutamate receptors as seen by light: spectroscopic studies of structure-function relationships
title Glutamate receptors as seen by light: spectroscopic studies of structure-function relationships
spellingShingle Glutamate receptors as seen by light: spectroscopic studies of structure-function relationships
Mankiewicz,K.A.
Vibrational spectroscopy
Fluorescence resonance energy transfer
a-Amino-3-hydroxy- 5-methyl-4- isoxazolepropionic acid receptors
Agonist activation
Ligand binding
title_short Glutamate receptors as seen by light: spectroscopic studies of structure-function relationships
title_full Glutamate receptors as seen by light: spectroscopic studies of structure-function relationships
title_fullStr Glutamate receptors as seen by light: spectroscopic studies of structure-function relationships
title_full_unstemmed Glutamate receptors as seen by light: spectroscopic studies of structure-function relationships
title_sort Glutamate receptors as seen by light: spectroscopic studies of structure-function relationships
author Mankiewicz,K.A.
author_facet Mankiewicz,K.A.
Jayaraman,V.
author_role author
author2 Jayaraman,V.
author2_role author
dc.contributor.author.fl_str_mv Mankiewicz,K.A.
Jayaraman,V.
dc.subject.por.fl_str_mv Vibrational spectroscopy
Fluorescence resonance energy transfer
a-Amino-3-hydroxy- 5-methyl-4- isoxazolepropionic acid receptors
Agonist activation
Ligand binding
topic Vibrational spectroscopy
Fluorescence resonance energy transfer
a-Amino-3-hydroxy- 5-methyl-4- isoxazolepropionic acid receptors
Agonist activation
Ligand binding
description Ionotropic glutamate receptors are major excitatory receptors in the central nervous system and also have a far reaching influence in other areas of the body. Their modular nature has allowed for the isolation of the ligand-binding domain and for subsequent structural studies using a variety of spectroscopic techniques. This review will discuss the role of specific ligand:protein interactions in mediating activation in the a-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid subtype of glutamate receptors as established by various spectroscopic investigations of the GluR2 and GluR4 subunits of this receptor. Specifically, this review will provide an introduction to the insight gained from X-ray crystallography and nuclear magnetic resonance investigations and then go on to focus on studies utilizing vibrational spectroscopy and fluorescence resonance energy transfer to study the behavior of the isolated ligand-binding domain in solution and discuss the importance of specific ligand:protein interactions in the mechanism of receptor activation.
publishDate 2007
dc.date.none.fl_str_mv 2007-11-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2007001100001
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2007001100001
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0100-879X2007001100001
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Associação Brasileira de Divulgação Científica
publisher.none.fl_str_mv Associação Brasileira de Divulgação Científica
dc.source.none.fl_str_mv Brazilian Journal of Medical and Biological Research v.40 n.11 2007
reponame:Brazilian Journal of Medical and Biological Research
instname:Associação Brasileira de Divulgação Científica (ABDC)
instacron:ABDC
instname_str Associação Brasileira de Divulgação Científica (ABDC)
instacron_str ABDC
institution ABDC
reponame_str Brazilian Journal of Medical and Biological Research
collection Brazilian Journal of Medical and Biological Research
repository.name.fl_str_mv Brazilian Journal of Medical and Biological Research - Associação Brasileira de Divulgação Científica (ABDC)
repository.mail.fl_str_mv bjournal@terra.com.br||bjournal@terra.com.br
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