Phospholipase A(2) Inhibitors from Snake Blood (sbPLIs)
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , , , , , , |
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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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 |
|
_version_ |
1808129103173255168 |