Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Repositório Institucional da FIOCRUZ (ARCA) |
Texto Completo: | https://www.arca.fiocruz.br/handle/icict/15602 |
Resumo: | FAPESP, CNPq, TWAS, DAAD, CAPES |
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Ullah, AnwarSouza, Tatiana de Arruda Campos Brasil deZanphorlin, Leticia MariaMariutti, Ricardo B.Santana, V. S.Murakami, Mario TyagoArni, R. K.2016-09-02T19:10:05Z2016-09-02T19:10:05Z2012ULLAH, Anwar et al. Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes. Protein Science, v. 22, n. 1, p. 128-132, 2012.0961-8368https://www.arca.fiocruz.br/handle/icict/1560210.1002/pro.2189FAPESP, CNPq, TWAS, DAAD, CAPESUniversidade Estadual Paulista. Instituto de Biociências Letras e Ciências Exatas. Departamento de Física. Centro Multiusuário de Inovação Biomolecular, São Jose do Rio Preto, SP, Brasil.Centro Nacional de Pesquisa em Energia e Materiais. Laboratório Nacional de Biociências. Campinas, SP, Brasil / Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.Universidade Estadual Paulista. Instituto de Biociências Letras e Ciências Exatas. Departamento de Física. Centro Multiusuário de Inovação Biomolecular, São Jose do Rio Preto, SP, Brasil.Universidade Estadual Paulista. Instituto de Biociências Letras e Ciências Exatas. Departamento de Física. Centro Multiusuário de Inovação Biomolecular, São Jose do Rio Preto, SP, Brasil.Universidade Estadual Paulista. Instituto de Biociências Letras e Ciências Exatas. Departamento de Física. Centro Multiusuário de Inovação Biomolecular, São Jose do Rio Preto, SP, Brasil.Centro Nacional de Pesquisa em Energia e Materiais. Laboratório Nacional de Biociências. Campinas, SP, Brasil.Universidade Estadual Paulista. Instituto de Biociências Letras e Ciências Exatas. Departamento de Física. Centro Multiusuário de Inovação Biomolecular, São Jose do Rio Preto, SP, Brasil.Snake venom serine proteinases (SVSPs) are hemostatically active toxins that perturb the maintenance and regulation of both the blood coagulation cascade and fibrinolytic feedback system at specific points, and hence, are widely used as tools in pharmacological and clinical diagnosis. The crystal structure of a thrombin-like enzyme (TLE) from Bothrops jararacussu venom (Jararacussin-I) was determined at 2.48 Å resolution. This is the first crystal structure of a TLE and allows structural comparisons with both the Agkistrodon contortrix contortrix Protein C Activator and the Trimeresurus stejnegeri plasminogen activator. Despite the highly conserved overall fold, significant differences in the amino acid compositions and three-dimensional conformations of the loops surrounding the active site significantly alter the molecular topography and charge distribution profile of the catalytic interface. In contrast to other SVSPs, the catalytic interface of Jararacussin-I is highly negatively charged, which contributes to its unique macromolecular selectivity.porCrystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleJararacussin-IThrombin-like enzymeBothrops jararacussuCrystal structureProteinsProteínasReceptores de TrombinaVenenos de Serpentesinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da FIOCRUZ (ARCA)instname:Fundação Oswaldo Cruz (FIOCRUZ)instacron:FIOCRUZLICENSElicense.txtlicense.txttext/plain; charset=utf-83074https://www.arca.fiocruz.br/bitstream/icict/15602/1/license.txt0271fb68963c017aa933c7aff60379f4MD51ORIGINALCrystal structure of Jararacussin-I.pdfCrystal structure of Jararacussin-I.pdfapplication/pdf356808https://www.arca.fiocruz.br/bitstream/icict/15602/2/Crystal%20structure%20of%20Jararacussin-I.pdfcd01e76570df32e71244d77604645768MD52TEXTCrystal structure of Jararacussin-I.pdf.txtCrystal structure of Jararacussin-I.pdf.txtExtracted texttext/plain20677https://www.arca.fiocruz.br/bitstream/icict/15602/3/Crystal%20structure%20of%20Jararacussin-I.pdf.txt23cb3194dcccd9ee15466b5b34b5b42fMD53icict/156022019-11-23 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dc.title.pt_BR.fl_str_mv |
Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes |
title |
Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes |
spellingShingle |
Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes Ullah, Anwar Jararacussin-I Thrombin-like enzyme Bothrops jararacussu Crystal structure Proteins Proteínas Receptores de Trombina Venenos de Serpentes |
title_short |
Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes |
title_full |
Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes |
title_fullStr |
Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes |
title_full_unstemmed |
Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes |
title_sort |
Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes |
author |
Ullah, Anwar |
author_facet |
Ullah, Anwar Souza, Tatiana de Arruda Campos Brasil de Zanphorlin, Leticia Maria Mariutti, Ricardo B. Santana, V. S. Murakami, Mario Tyago Arni, R. K. |
author_role |
author |
author2 |
Souza, Tatiana de Arruda Campos Brasil de Zanphorlin, Leticia Maria Mariutti, Ricardo B. Santana, V. S. Murakami, Mario Tyago Arni, R. K. |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Ullah, Anwar Souza, Tatiana de Arruda Campos Brasil de Zanphorlin, Leticia Maria Mariutti, Ricardo B. Santana, V. S. Murakami, Mario Tyago Arni, R. K. |
dc.subject.en.pt_BR.fl_str_mv |
Jararacussin-I Thrombin-like enzyme Bothrops jararacussu Crystal structure |
topic |
Jararacussin-I Thrombin-like enzyme Bothrops jararacussu Crystal structure Proteins Proteínas Receptores de Trombina Venenos de Serpentes |
dc.subject.decs.En.fl_str_mv |
Proteins |
dc.subject.decs.pt_BR.fl_str_mv |
Proteínas Receptores de Trombina Venenos de Serpentes |
description |
FAPESP, CNPq, TWAS, DAAD, CAPES |
publishDate |
2012 |
dc.date.issued.fl_str_mv |
2012 |
dc.date.accessioned.fl_str_mv |
2016-09-02T19:10:05Z |
dc.date.available.fl_str_mv |
2016-09-02T19:10:05Z |
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.citation.fl_str_mv |
ULLAH, Anwar et al. Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes. Protein Science, v. 22, n. 1, p. 128-132, 2012. |
dc.identifier.uri.fl_str_mv |
https://www.arca.fiocruz.br/handle/icict/15602 |
dc.identifier.issn.pt_BR.fl_str_mv |
0961-8368 |
dc.identifier.doi.pt_BR.fl_str_mv |
10.1002/pro.2189 |
identifier_str_mv |
ULLAH, Anwar et al. Crystal structure of Jararacussin-I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes. Protein Science, v. 22, n. 1, p. 128-132, 2012. 0961-8368 10.1002/pro.2189 |
url |
https://www.arca.fiocruz.br/handle/icict/15602 |
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por |
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por |
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info:eu-repo/semantics/openAccess |
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openAccess |
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