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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

Springer Verlag

Manager: Ministerio de Ciencia e Innovación (Espanya)
Author: Serrano, Soraya
Callís Figueres, Mariona
Vilanova i Brugués, Maria
Benito i Mundet, Antoni
Laurents, Douglas V.
Ribó i Panosa, Marc
Bruix, Marta
Abstract: 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
Document access: http://hdl.handle.net/2072/297265
Language: eng
Publisher: Springer Verlag
Rights: Tots els drets reservats
Subject: Enginyeria de proteïnes
Protein engineering
Enzims
Enzymes
Title: 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen
Type: info:eu-repo/semantics/article
Repository: Recercat

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