Phospholipase A(2) Inhibitors from Snake Blood (sbPLIs)

Detalhes bibliográficos
Autor(a) principal: Fortes-Dias, Consuelo L.
Data de Publicação: 2017
Outros Autores: Campos, Patricia Cota, Fernandes, Carlos Alexandre H. [UNESP], Fontes, Marcos Roberto M. [UNESP], Inagaki, H., Vogel, C. W., Mukherjee, A. K., Rahmy, T. R., Gopalakrishnakone, P.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1007/978-94-007-6410-1_33
http://hdl.handle.net/11449/245406
Resumo: Several snake species have been naturally provided with protein inhibitors with the primary aim of self-protection against the eventual presence of venom toxins in their circulating blood. Phospholipase A(2) inhibitors are among the most studied molecules in that group. Such molecules have been identified in venomous and nonvenomous snake species and are generally known as sbPLIs (which stand for snake blood phospholipase A(2) inhibitors). Based on the presence of known domains of mammalian proteins, sbPLIs may belong to any of three structural classes (alpha, beta, or gamma). All the domains are involved in protein-protein interactions. The sbaPLIs present a characteristic C-type lectin-like domain (CTLD) highly similar to the carbohydrate recognition domain (CRD) of Ca2+-dependent lectins, which includes mannose-binding and lung surfactants A and D (SP-A and SP-D) proteins. Beta-type inhibitors (sb beta PLIs) are characterized by the presence of nine tandem leucine-rich repeats (LRRs), whereas sb.PLIs share the characteristic three-finger motifs of the Ly-6 family, CD59 and the urokinase-type plasminogen activator (u-PAR). Despite of no crystallographic data of sbPLIs, several computational and biophysical techniques have been applied, in an effort to provide structural data for structure-function relationships between these inhibitors and svPLAs. This chapter will be devoted to a brief but not extensive review of general aspects, quaternary structures, molecular mechanisms, and applications of sbPLIs.
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spelling Phospholipase A(2) Inhibitors from Snake Blood (sbPLIs)Phospholipase A(2)PLA(2)PLA(2) inhibitorsbPLISnakeSeveral snake species have been naturally provided with protein inhibitors with the primary aim of self-protection against the eventual presence of venom toxins in their circulating blood. Phospholipase A(2) inhibitors are among the most studied molecules in that group. Such molecules have been identified in venomous and nonvenomous snake species and are generally known as sbPLIs (which stand for snake blood phospholipase A(2) inhibitors). Based on the presence of known domains of mammalian proteins, sbPLIs may belong to any of three structural classes (alpha, beta, or gamma). All the domains are involved in protein-protein interactions. The sbaPLIs present a characteristic C-type lectin-like domain (CTLD) highly similar to the carbohydrate recognition domain (CRD) of Ca2+-dependent lectins, which includes mannose-binding and lung surfactants A and D (SP-A and SP-D) proteins. Beta-type inhibitors (sb beta PLIs) are characterized by the presence of nine tandem leucine-rich repeats (LRRs), whereas sb.PLIs share the characteristic three-finger motifs of the Ly-6 family, CD59 and the urokinase-type plasminogen activator (u-PAR). Despite of no crystallographic data of sbPLIs, several computational and biophysical techniques have been applied, in an effort to provide structural data for structure-function relationships between these inhibitors and svPLAs. This chapter will be devoted to a brief but not extensive review of general aspects, quaternary structures, molecular mechanisms, and applications of sbPLIs.Fundacao Ezequiel Dias, Lab Enzimol Aplicada Diretoria Pesquisa & Desenvo, Belo Horizonte, MG, BrazilUniv Estadual Paulista UNESP, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP, BrazilUniv Estadual Paulista UNESP, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP, BrazilSpringerFundacao Ezequiel DiasUniversidade Estadual Paulista (UNESP)Fortes-Dias, Consuelo L.Campos, Patricia CotaFernandes, Carlos Alexandre H. [UNESP]Fontes, Marcos Roberto M. [UNESP]Inagaki, H.Vogel, C. W.Mukherjee, A. K.Rahmy, T. R.Gopalakrishnakone, P.2023-07-29T11:53:55Z2023-07-29T11:53:55Z2017-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article105-122http://dx.doi.org/10.1007/978-94-007-6410-1_33Snake Venoms. Dordrecht: Springer, p. 105-122, 2017.2542-761Xhttp://hdl.handle.net/11449/24540610.1007/978-94-007-6410-1_33WOS:000415218800007Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengSnake Venomsinfo:eu-repo/semantics/openAccess2023-07-29T11:53:55Zoai:repositorio.unesp.br:11449/245406Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T19:39:47.664151Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Phospholipase A(2) Inhibitors from Snake Blood (sbPLIs)
title Phospholipase A(2) Inhibitors from Snake Blood (sbPLIs)
spellingShingle Phospholipase A(2) Inhibitors from Snake Blood (sbPLIs)
Fortes-Dias, Consuelo L.
Phospholipase A(2)
PLA(2)
PLA(2) inhibitor
sbPLI
Snake
title_short Phospholipase A(2) Inhibitors from Snake Blood (sbPLIs)
title_full Phospholipase A(2) Inhibitors from Snake Blood (sbPLIs)
title_fullStr Phospholipase A(2) Inhibitors from Snake Blood (sbPLIs)
title_full_unstemmed Phospholipase A(2) Inhibitors from Snake Blood (sbPLIs)
title_sort Phospholipase A(2) Inhibitors from Snake Blood (sbPLIs)
author Fortes-Dias, Consuelo L.
author_facet Fortes-Dias, Consuelo L.
Campos, Patricia Cota
Fernandes, Carlos Alexandre H. [UNESP]
Fontes, Marcos Roberto M. [UNESP]
Inagaki, H.
Vogel, C. W.
Mukherjee, A. K.
Rahmy, T. R.
Gopalakrishnakone, P.
author_role author
author2 Campos, Patricia Cota
Fernandes, Carlos Alexandre H. [UNESP]
Fontes, Marcos Roberto M. [UNESP]
Inagaki, H.
Vogel, C. W.
Mukherjee, A. K.
Rahmy, T. R.
Gopalakrishnakone, P.
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Fundacao Ezequiel Dias
Universidade Estadual Paulista (UNESP)
dc.contributor.author.fl_str_mv Fortes-Dias, Consuelo L.
Campos, Patricia Cota
Fernandes, Carlos Alexandre H. [UNESP]
Fontes, Marcos Roberto M. [UNESP]
Inagaki, H.
Vogel, C. W.
Mukherjee, A. K.
Rahmy, T. R.
Gopalakrishnakone, P.
dc.subject.por.fl_str_mv Phospholipase A(2)
PLA(2)
PLA(2) inhibitor
sbPLI
Snake
topic Phospholipase A(2)
PLA(2)
PLA(2) inhibitor
sbPLI
Snake
description Several snake species have been naturally provided with protein inhibitors with the primary aim of self-protection against the eventual presence of venom toxins in their circulating blood. Phospholipase A(2) inhibitors are among the most studied molecules in that group. Such molecules have been identified in venomous and nonvenomous snake species and are generally known as sbPLIs (which stand for snake blood phospholipase A(2) inhibitors). Based on the presence of known domains of mammalian proteins, sbPLIs may belong to any of three structural classes (alpha, beta, or gamma). All the domains are involved in protein-protein interactions. The sbaPLIs present a characteristic C-type lectin-like domain (CTLD) highly similar to the carbohydrate recognition domain (CRD) of Ca2+-dependent lectins, which includes mannose-binding and lung surfactants A and D (SP-A and SP-D) proteins. Beta-type inhibitors (sb beta PLIs) are characterized by the presence of nine tandem leucine-rich repeats (LRRs), whereas sb.PLIs share the characteristic three-finger motifs of the Ly-6 family, CD59 and the urokinase-type plasminogen activator (u-PAR). Despite of no crystallographic data of sbPLIs, several computational and biophysical techniques have been applied, in an effort to provide structural data for structure-function relationships between these inhibitors and svPLAs. This chapter will be devoted to a brief but not extensive review of general aspects, quaternary structures, molecular mechanisms, and applications of sbPLIs.
publishDate 2017
dc.date.none.fl_str_mv 2017-01-01
2023-07-29T11:53:55Z
2023-07-29T11:53:55Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1007/978-94-007-6410-1_33
Snake Venoms. Dordrecht: Springer, p. 105-122, 2017.
2542-761X
http://hdl.handle.net/11449/245406
10.1007/978-94-007-6410-1_33
WOS:000415218800007
url http://dx.doi.org/10.1007/978-94-007-6410-1_33
http://hdl.handle.net/11449/245406
identifier_str_mv Snake Venoms. Dordrecht: Springer, p. 105-122, 2017.
2542-761X
10.1007/978-94-007-6410-1_33
WOS:000415218800007
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Snake Venoms
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 105-122
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
dc.source.none.fl_str_mv Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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