1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen

Onconase® FL-G zymogen is a 120 residue protein produced by circular permutation of the native Onconase® sequence. In this construction, the wild type N- and C-termini are linked by a 16 residue segment and new N- and C-termini are generated at wild type positions R73 and S72. This novel segment lin...

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Detalles Bibliográficos
Autores: Serrano, Soraya, Callís Figueres, Mariona, Vilanova i Brugués, Maria, Benito i Mundet, Antoni, Laurents, Douglas V., Ribó i Panosa, Marc, Bruix, Marta
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2013
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10256/11967
Acceso en línea:http://hdl.handle.net/10256/11967
Access Level:acceso embargado
Palabra clave:Enginyeria de proteïnes
Protein engineering
Enzims
Enzymes
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spelling 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogenSerrano, SorayaCallís Figueres, MarionaVilanova i Brugués, MariaBenito i Mundet, AntoniLaurents, Douglas V.Ribó i Panosa, MarcBruix, MartaEnginyeria de proteïnesProtein engineeringEnzimsEnzymesOnconase® FL-G zymogen is a 120 residue protein produced by circular permutation of the native Onconase® sequence. In this construction, the wild type N- and C-termini are linked by a 16 residue segment and new N- and C-termini are generated at wild type positions R73 and S72. This novel segment linking the native N- and C-termini is designed to obstruct Onconase's® active site and encloses a cleavage site for the HIV-1 protease. As a first step towards the resolution of its 3D structure and the study of its structure-function relationships, we report here the nearly complete NMR 1H, 13C and 15N resonance chemical shift assignments at pH 5.2 and 35 C (BMRB deposit no 17973). The results presented here clearly show that the structure of the wild type Onconase ® is conserved in the FL-G zymogenThis work was supported by the projects, CTQ2008-0080, CTQ2010-21567-C02-02 and BFU2009-06935/ BMC from MICINN and PUG2008A from the Universitat de GironaSpringerMinisterio de Ciencia e Innovación (Espanya)info2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10256/11967© Biomolecular NMR Assignments, 2013, vol. 7, p. 13-15Articles publicats (D-B)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)Inglésinfo:eu-repo/semantics/altIdentifier/doi/10.1007/s12104-012-9367-0info:eu-repo/semantics/altIdentifier/issn/1874-2718info:eu-repo/semantics/altIdentifier/eissn/1874-270Xinfo:eu-repo/grantAgreement/MICINN//BFU2009-06935Tots els drets reservatsinfo:eu-repo/semantics/embargoedAccessoai:recercat.cat:10256/119672026-05-29T05:05:01Z
dc.title.none.fl_str_mv 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen
title 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen
spellingShingle 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen
Serrano, Soraya
Enginyeria de proteïnes
Protein engineering
Enzims
Enzymes
title_short 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen
title_full 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen
title_fullStr 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen
title_full_unstemmed 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen
title_sort 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen
dc.creator.none.fl_str_mv Serrano, Soraya
Callís Figueres, Mariona
Vilanova i Brugués, Maria
Benito i Mundet, Antoni
Laurents, Douglas V.
Ribó i Panosa, Marc
Bruix, Marta
author Serrano, Soraya
author_facet Serrano, Soraya
Callís Figueres, Mariona
Vilanova i Brugués, Maria
Benito i Mundet, Antoni
Laurents, Douglas V.
Ribó i Panosa, Marc
Bruix, Marta
author_role author
author2 Callís Figueres, Mariona
Vilanova i Brugués, Maria
Benito i Mundet, Antoni
Laurents, Douglas V.
Ribó i Panosa, Marc
Bruix, Marta
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia e Innovación (Espanya)
dc.subject.none.fl_str_mv Enginyeria de proteïnes
Protein engineering
Enzims
Enzymes
topic Enginyeria de proteïnes
Protein engineering
Enzims
Enzymes
description Onconase® FL-G zymogen is a 120 residue protein produced by circular permutation of the native Onconase® sequence. In this construction, the wild type N- and C-termini are linked by a 16 residue segment and new N- and C-termini are generated at wild type positions R73 and S72. This novel segment linking the native N- and C-termini is designed to obstruct Onconase's® active site and encloses a cleavage site for the HIV-1 protease. As a first step towards the resolution of its 3D structure and the study of its structure-function relationships, we report here the nearly complete NMR 1H, 13C and 15N resonance chemical shift assignments at pH 5.2 and 35 C (BMRB deposit no 17973). The results presented here clearly show that the structure of the wild type Onconase ® is conserved in the FL-G zymogen
publishDate 2013
dc.date.none.fl_str_mv 2013
info
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10256/11967
url http://hdl.handle.net/10256/11967
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1007/s12104-012-9367-0
info:eu-repo/semantics/altIdentifier/issn/1874-2718
info:eu-repo/semantics/altIdentifier/eissn/1874-270X
info:eu-repo/grantAgreement/MICINN//BFU2009-06935
dc.rights.none.fl_str_mv Tots els drets reservats
info:eu-repo/semantics/embargoedAccess
rights_invalid_str_mv Tots els drets reservats
eu_rights_str_mv embargoedAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
dc.source.none.fl_str_mv © Biomolecular NMR Assignments, 2013, vol. 7, p. 13-15
Articles publicats (D-B)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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