α-Conotoxins

Autores
Arias, Hugo Rubén; Blanton, Michael P
Año de publicación
2000
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
α-Conotoxins (α-CgTxs) are a family of Cys-enriched peptides found in several marine snails from the genus Conus. These small peptides behave pharmacologically as competitive antagonists of the nicotinic acetylcholine receptor (AChR). The data indicate that (1) α-CgTxs are able to discriminate between muscle- and neuronal-type AChRs and even among distinct AChR subtypes; (2) the binding sites for α-CgTxs are located, like other cholinergic ligands, at the interface of α and non-α subunits (γ, δ, and ε for the muscle-type AChR, and β for several neuronal-type AChRs); (3) some α-CgTxs differentiate the high- from the low-affinity binding site found on either α/non-α subunit interface; and that (4) specific residues in the cholinergic binding site are energetically coupled with their corresponding pairs in the toxin stabilizing the α-CgTx-AChR complex. The α-CgTxs have proven to be excellent probes for studying the structure and function of the AChR family.
Fil: Arias, Hugo Rubén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Matemática Bahía Blanca. Universidad Nacional del Sur. Departamento de Matemática. Instituto de Matemática Bahía Blanca; Argentina. Texas Teach University Health Sciences Center; Estados Unidos
Fil: Blanton, Michael P. Texas Teach University Health Sciences Center; Estados Unidos
Materia
Α-Conotoxins
Competitive Antagonists
Nicotinic Acetylcholine Receptors
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/78993

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network_name_str CONICET Digital (CONICET)
spelling α-ConotoxinsArias, Hugo RubénBlanton, Michael PΑ-ConotoxinsCompetitive AntagonistsNicotinic Acetylcholine Receptorshttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3α-Conotoxins (α-CgTxs) are a family of Cys-enriched peptides found in several marine snails from the genus Conus. These small peptides behave pharmacologically as competitive antagonists of the nicotinic acetylcholine receptor (AChR). The data indicate that (1) α-CgTxs are able to discriminate between muscle- and neuronal-type AChRs and even among distinct AChR subtypes; (2) the binding sites for α-CgTxs are located, like other cholinergic ligands, at the interface of α and non-α subunits (γ, δ, and ε for the muscle-type AChR, and β for several neuronal-type AChRs); (3) some α-CgTxs differentiate the high- from the low-affinity binding site found on either α/non-α subunit interface; and that (4) specific residues in the cholinergic binding site are energetically coupled with their corresponding pairs in the toxin stabilizing the α-CgTx-AChR complex. The α-CgTxs have proven to be excellent probes for studying the structure and function of the AChR family.Fil: Arias, Hugo Rubén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Matemática Bahía Blanca. Universidad Nacional del Sur. Departamento de Matemática. Instituto de Matemática Bahía Blanca; Argentina. Texas Teach University Health Sciences Center; Estados UnidosFil: Blanton, Michael P. Texas Teach University Health Sciences Center; Estados UnidosPergamon-Elsevier Science Ltd2000-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/78993Arias, Hugo Rubén; Blanton, Michael P; α-Conotoxins; Pergamon-Elsevier Science Ltd; International Journal of Biochemistry and Cellular Biology; 32; 10; 8-2000; 1017-10281357-2725CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1357272500000510?via%3Dihubinfo:eu-repo/semantics/altIdentifier/doi/10.1016/S1357-2725(00)00051-0info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:29:52Zoai:ri.conicet.gov.ar:11336/78993instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:29:52.798CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv α-Conotoxins
title α-Conotoxins
spellingShingle α-Conotoxins
Arias, Hugo Rubén
Α-Conotoxins
Competitive Antagonists
Nicotinic Acetylcholine Receptors
title_short α-Conotoxins
title_full α-Conotoxins
title_fullStr α-Conotoxins
title_full_unstemmed α-Conotoxins
title_sort α-Conotoxins
dc.creator.none.fl_str_mv Arias, Hugo Rubén
Blanton, Michael P
author Arias, Hugo Rubén
author_facet Arias, Hugo Rubén
Blanton, Michael P
author_role author
author2 Blanton, Michael P
author2_role author
dc.subject.none.fl_str_mv Α-Conotoxins
Competitive Antagonists
Nicotinic Acetylcholine Receptors
topic Α-Conotoxins
Competitive Antagonists
Nicotinic Acetylcholine Receptors
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv α-Conotoxins (α-CgTxs) are a family of Cys-enriched peptides found in several marine snails from the genus Conus. These small peptides behave pharmacologically as competitive antagonists of the nicotinic acetylcholine receptor (AChR). The data indicate that (1) α-CgTxs are able to discriminate between muscle- and neuronal-type AChRs and even among distinct AChR subtypes; (2) the binding sites for α-CgTxs are located, like other cholinergic ligands, at the interface of α and non-α subunits (γ, δ, and ε for the muscle-type AChR, and β for several neuronal-type AChRs); (3) some α-CgTxs differentiate the high- from the low-affinity binding site found on either α/non-α subunit interface; and that (4) specific residues in the cholinergic binding site are energetically coupled with their corresponding pairs in the toxin stabilizing the α-CgTx-AChR complex. The α-CgTxs have proven to be excellent probes for studying the structure and function of the AChR family.
Fil: Arias, Hugo Rubén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Matemática Bahía Blanca. Universidad Nacional del Sur. Departamento de Matemática. Instituto de Matemática Bahía Blanca; Argentina. Texas Teach University Health Sciences Center; Estados Unidos
Fil: Blanton, Michael P. Texas Teach University Health Sciences Center; Estados Unidos
description α-Conotoxins (α-CgTxs) are a family of Cys-enriched peptides found in several marine snails from the genus Conus. These small peptides behave pharmacologically as competitive antagonists of the nicotinic acetylcholine receptor (AChR). The data indicate that (1) α-CgTxs are able to discriminate between muscle- and neuronal-type AChRs and even among distinct AChR subtypes; (2) the binding sites for α-CgTxs are located, like other cholinergic ligands, at the interface of α and non-α subunits (γ, δ, and ε for the muscle-type AChR, and β for several neuronal-type AChRs); (3) some α-CgTxs differentiate the high- from the low-affinity binding site found on either α/non-α subunit interface; and that (4) specific residues in the cholinergic binding site are energetically coupled with their corresponding pairs in the toxin stabilizing the α-CgTx-AChR complex. The α-CgTxs have proven to be excellent probes for studying the structure and function of the AChR family.
publishDate 2000
dc.date.none.fl_str_mv 2000-08
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/78993
Arias, Hugo Rubén; Blanton, Michael P; α-Conotoxins; Pergamon-Elsevier Science Ltd; International Journal of Biochemistry and Cellular Biology; 32; 10; 8-2000; 1017-1028
1357-2725
CONICET Digital
CONICET
url http://hdl.handle.net/11336/78993
identifier_str_mv Arias, Hugo Rubén; Blanton, Michael P; α-Conotoxins; Pergamon-Elsevier Science Ltd; International Journal of Biochemistry and Cellular Biology; 32; 10; 8-2000; 1017-1028
1357-2725
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1357272500000510?via%3Dihub
info:eu-repo/semantics/altIdentifier/doi/10.1016/S1357-2725(00)00051-0
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Pergamon-Elsevier Science Ltd
publisher.none.fl_str_mv Pergamon-Elsevier Science Ltd
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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