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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 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

This work was supported by the projects, CTQ2008-0080, CTQ2010-21567-C02-02 and BFU2009-06935/ BMC from MICINN and PUG2008A from the Universitat de Girona

© Biomolecular NMR Assignments, 2013, vol. 7, p. 13-15

Springer Verlag

Director: Ministerio de Ciencia e Innovación (Espanya)
Autor: Serrano, Soraya
Callís Figueres, Mariona
Vilanova i Brugués, Maria
Benito i Mundet, Antoni
Laurents, Douglas V.
Ribó i Panosa, Marc
Bruix, Marta
Data: 2013
Resum: 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
This work was supported by the projects, CTQ2008-0080, CTQ2010-21567-C02-02 and BFU2009-06935/ BMC from MICINN and PUG2008A from the Universitat de Girona
Format: application/pdf
Cita: 017120
ISSN: 1874-2718 (versió paper)
1874-270X (versió electrònica)
Accés al document: http://hdl.handle.net/10256/11967
Llenguatge: eng
Editor: Springer Verlag
Col·lecció: MICINN/PN 2010-2012/BFU2009-06935
Reproducció digital del document publicat a: http://dx.doi.org/10.1007/s12104-012-9367-0
Articles publicats (D-B)
És part de: © Biomolecular NMR Assignments, 2013, vol. 7, p. 13-15
Drets: Tots els drets reservats
Matèria: Enginyeria de proteïnes
Protein engineering
Enzims
Enzymes
Títol: 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen
Tipus: info:eu-repo/semantics/article
Repositori: DUGiDocs

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