Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor
Autor(a) principal: | |
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Data de Publicação: | 2007 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10316/3858 https://doi.org/10.1016/j.bbrc.2007.06.144 |
Resumo: | Bauhinia bauhinioides Cruzipain Inhibitor (BbCI) is a cysteine protease inhibitor highly homologous to plant Kunitz-type inhibitors. However, in contrast to classical Kunitz family inhibitors it lacks cysteine residues and therefore disulfide bridges. BbCI is also distinct in the ability to inactivate enzymes belonging to two different classes, cysteine and serine proteases. Besides inhibiting the cysteine protease cruzipain, BbCI also inhibits cathepsin L and the serine proteases HNE (human neutrophil elastase) and PPE (porcine pancreatic elastase). Monoclinic crystals of the recombinant inhibitor that diffract to 1.7 Å resolution were obtained using hanging drop method by vapor diffusion at 18 °C. The refined structure shows the conservative [beta]-trefoil fold features of the Kunitz inhibitors. In BbCI, one of the two characteristic S-S bonds is replaced by the water-mediated interaction between Tyr125 and Gly132. In this work we explore the structural differences between Kunitz-type inhibitors and analyze the essential interactions that maintain the protein structural stability preserving its biological function. |
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Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitorCathepsinCrystallographyCruzipainElastaseKallikreinKunitz protease inhibitorsX-ray diffractionBauhinia bauhinioides Cruzipain Inhibitor (BbCI) is a cysteine protease inhibitor highly homologous to plant Kunitz-type inhibitors. However, in contrast to classical Kunitz family inhibitors it lacks cysteine residues and therefore disulfide bridges. BbCI is also distinct in the ability to inactivate enzymes belonging to two different classes, cysteine and serine proteases. Besides inhibiting the cysteine protease cruzipain, BbCI also inhibits cathepsin L and the serine proteases HNE (human neutrophil elastase) and PPE (porcine pancreatic elastase). Monoclinic crystals of the recombinant inhibitor that diffract to 1.7 Å resolution were obtained using hanging drop method by vapor diffusion at 18 °C. The refined structure shows the conservative [beta]-trefoil fold features of the Kunitz inhibitors. In BbCI, one of the two characteristic S-S bonds is replaced by the water-mediated interaction between Tyr125 and Gly132. In this work we explore the structural differences between Kunitz-type inhibitors and analyze the essential interactions that maintain the protein structural stability preserving its biological function.http://www.sciencedirect.com/science/article/B6WBK-4P48623-2/1/e9495eee44144f4581cfeca1164b43fd2007info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleaplication/PDFhttp://hdl.handle.net/10316/3858http://hdl.handle.net/10316/3858https://doi.org/10.1016/j.bbrc.2007.06.144engBiochemical and Biophysical Research Communications. 360:4 (2007) 735-740Hansen, DaianeMacedo-Ribeiro, SandraVeríssimo, PaulaYoo Im, SoniaSampaio, Misako UemuraOliva, Maria Luiza Vilelainfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2021-11-09T09:29:41ZPortal AgregadorONG |
dc.title.none.fl_str_mv |
Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor |
title |
Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor |
spellingShingle |
Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor Hansen, Daiane Cathepsin Crystallography Cruzipain Elastase Kallikrein Kunitz protease inhibitors X-ray diffraction |
title_short |
Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor |
title_full |
Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor |
title_fullStr |
Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor |
title_full_unstemmed |
Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor |
title_sort |
Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor |
author |
Hansen, Daiane |
author_facet |
Hansen, Daiane Macedo-Ribeiro, Sandra Veríssimo, Paula Yoo Im, Sonia Sampaio, Misako Uemura Oliva, Maria Luiza Vilela |
author_role |
author |
author2 |
Macedo-Ribeiro, Sandra Veríssimo, Paula Yoo Im, Sonia Sampaio, Misako Uemura Oliva, Maria Luiza Vilela |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Hansen, Daiane Macedo-Ribeiro, Sandra Veríssimo, Paula Yoo Im, Sonia Sampaio, Misako Uemura Oliva, Maria Luiza Vilela |
dc.subject.por.fl_str_mv |
Cathepsin Crystallography Cruzipain Elastase Kallikrein Kunitz protease inhibitors X-ray diffraction |
topic |
Cathepsin Crystallography Cruzipain Elastase Kallikrein Kunitz protease inhibitors X-ray diffraction |
description |
Bauhinia bauhinioides Cruzipain Inhibitor (BbCI) is a cysteine protease inhibitor highly homologous to plant Kunitz-type inhibitors. However, in contrast to classical Kunitz family inhibitors it lacks cysteine residues and therefore disulfide bridges. BbCI is also distinct in the ability to inactivate enzymes belonging to two different classes, cysteine and serine proteases. Besides inhibiting the cysteine protease cruzipain, BbCI also inhibits cathepsin L and the serine proteases HNE (human neutrophil elastase) and PPE (porcine pancreatic elastase). Monoclinic crystals of the recombinant inhibitor that diffract to 1.7 Å resolution were obtained using hanging drop method by vapor diffusion at 18 °C. The refined structure shows the conservative [beta]-trefoil fold features of the Kunitz inhibitors. In BbCI, one of the two characteristic S-S bonds is replaced by the water-mediated interaction between Tyr125 and Gly132. In this work we explore the structural differences between Kunitz-type inhibitors and analyze the essential interactions that maintain the protein structural stability preserving its biological function. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007 |
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://hdl.handle.net/10316/3858 http://hdl.handle.net/10316/3858 https://doi.org/10.1016/j.bbrc.2007.06.144 |
url |
http://hdl.handle.net/10316/3858 https://doi.org/10.1016/j.bbrc.2007.06.144 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Biochemical and Biophysical Research Communications. 360:4 (2007) 735-740 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
aplication/PDF |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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1777302656361955328 |