Structural foundations of sticholysin functionality

Actinoporins constitute a family of α pore-forming toxins produced by sea anemones. The soluble fold of these proteins consists of a β-sandwich flanked by two α-helices. Actinoporins exert their activity by specifically recognizing sphingomyelin at their target membranes. Once there, they penetrate...

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Detalles Bibliográficos
Autores: Palacios Ortega, Juan, García Linares, Sara, Rivera de Torre, Esperanza, Heras Márquez, Diego, Gavilanes, José G., Peter, Slotte, Martínez Del Pozo, Álvaro
Tipo de recurso: artículo
Fecha de publicación:2021
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/4870
Acceso en línea:https://hdl.handle.net/20.500.14352/4870
Access Level:acceso abierto
Palabra clave:577.1
577.2
actinoporins
lipid membranes
structure-function relationship
Biología molecular (Biología)
Bioquímica (Biología)
2415 Biología Molecular
2302 Bioquímica
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oai_identifier_str oai:docta.ucm.es:20.500.14352/4870
network_acronym_str ES
network_name_str España
repository_id_str
spelling Structural foundations of sticholysin functionalityPalacios Ortega, JuanGarcía Linares, SaraRivera de Torre, EsperanzaHeras Márquez, DiegoGavilanes, José G.Peter, SlotteMartínez Del Pozo, Álvaro577.1577.2actinoporinslipid membranesstructure-function relationshipBiología molecular (Biología)Bioquímica (Biología)2415 Biología Molecular2302 BioquímicaActinoporins constitute a family of α pore-forming toxins produced by sea anemones. The soluble fold of these proteins consists of a β-sandwich flanked by two α-helices. Actinoporins exert their activity by specifically recognizing sphingomyelin at their target membranes. Once there, they penetrate the membrane with their N-terminal α-helices, a process that leads to the formation of cation-selective pores. These pores kill the target cells by provoking an osmotic shock on them. In this review, we examine the role and relevance of the structural features of actinoporins, down to the residue level. We look at the specific amino acids that play significant roles in the function of actinoporins and their fold. Particular emphasis is given to those residues that display a high degree of conservation across the actinoporin sequences known to date. In light of the latest findings in the field, the membrane requirements for pore formation, the effect of lipid composition, and the process of pore formation are also discussed.ElsevierUniversidad Complutense de Madrid20212021-07-0820212021-07-08journal articlehttp://purl.org/coar/resource_type/c_6501info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/4870reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Atribución 3.0 Españahttps://creativecommons.org/licenses/by/3.0/es/info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/48702026-06-02T12:44:21Z
dc.title.none.fl_str_mv Structural foundations of sticholysin functionality
title Structural foundations of sticholysin functionality
spellingShingle Structural foundations of sticholysin functionality
Palacios Ortega, Juan
577.1
577.2
actinoporins
lipid membranes
structure-function relationship
Biología molecular (Biología)
Bioquímica (Biología)
2415 Biología Molecular
2302 Bioquímica
title_short Structural foundations of sticholysin functionality
title_full Structural foundations of sticholysin functionality
title_fullStr Structural foundations of sticholysin functionality
title_full_unstemmed Structural foundations of sticholysin functionality
title_sort Structural foundations of sticholysin functionality
dc.creator.none.fl_str_mv Palacios Ortega, Juan
García Linares, Sara
Rivera de Torre, Esperanza
Heras Márquez, Diego
Gavilanes, José G.
Peter, Slotte
Martínez Del Pozo, Álvaro
author Palacios Ortega, Juan
author_facet Palacios Ortega, Juan
García Linares, Sara
Rivera de Torre, Esperanza
Heras Márquez, Diego
Gavilanes, José G.
Peter, Slotte
Martínez Del Pozo, Álvaro
author_role author
author2 García Linares, Sara
Rivera de Torre, Esperanza
Heras Márquez, Diego
Gavilanes, José G.
Peter, Slotte
Martínez Del Pozo, Álvaro
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 577.1
577.2
actinoporins
lipid membranes
structure-function relationship
Biología molecular (Biología)
Bioquímica (Biología)
2415 Biología Molecular
2302 Bioquímica
topic 577.1
577.2
actinoporins
lipid membranes
structure-function relationship
Biología molecular (Biología)
Bioquímica (Biología)
2415 Biología Molecular
2302 Bioquímica
description Actinoporins constitute a family of α pore-forming toxins produced by sea anemones. The soluble fold of these proteins consists of a β-sandwich flanked by two α-helices. Actinoporins exert their activity by specifically recognizing sphingomyelin at their target membranes. Once there, they penetrate the membrane with their N-terminal α-helices, a process that leads to the formation of cation-selective pores. These pores kill the target cells by provoking an osmotic shock on them. In this review, we examine the role and relevance of the structural features of actinoporins, down to the residue level. We look at the specific amino acids that play significant roles in the function of actinoporins and their fold. Particular emphasis is given to those residues that display a high degree of conservation across the actinoporin sequences known to date. In light of the latest findings in the field, the membrane requirements for pore formation, the effect of lipid composition, and the process of pore formation are also discussed.
publishDate 2021
dc.date.none.fl_str_mv 2021
2021-07-08
2021
2021-07-08
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/4870
url https://hdl.handle.net/20.500.14352/4870
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución 3.0 España
https://creativecommons.org/licenses/by/3.0/es/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución 3.0 España
https://creativecommons.org/licenses/by/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,301629

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