title: (1)H, (13)C and (15)N resonance assignments of the Onconase FL-G zymogen.
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 (1)H, (13)C and (15)N 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.
authors.affiliation: Instituto de Química Física Rocasolano, Consejo Superior de Investigaciones Científicas, Serrano 119, 28006, Madrid, Spain.
authors.forename: Soraya
authors.initials: S
authors.lastname: Serrano
authors.forename: Mariona
authors.initials: M
authors.lastname: Callís
authors.forename: Maria
authors.initials: M
authors.lastname: Vilanova
authors.forename: Antoni
authors.initials: A
authors.lastname: Benito
authors.forename: Douglas V
authors.initials: DV
authors.lastname: Laurents
authors.forename: Marc
authors.initials: M
authors.lastname: Ribó
authors.forename: Marta
authors.initials: M
authors.lastname: Bruix
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D004792:Enzyme Precursors / Q000737:chemistry* / Q000378:metabolism; D016333:HIV Protease / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D012260:Ribonucleases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D004792:Enzyme Precursors; D012260:Ribonucleases; D016333:HIV Protease; C514803:p16 protease, Human immunodeficiency virus 1; C058703:ranpirnase