2LT5
Zymogen-FLG of the onconase
Summary for 2LT5
| Entry DOI | 10.2210/pdb2lt5/pdb |
| NMR Information | BMRB: 17973 |
| Descriptor | Protein P-30 (1 entity in total) |
| Functional Keywords | ribonuclease, hydrolase |
| Biological source | Rana pipiens (Northern leopard frog) |
| Total number of polymer chains | 1 |
| Total formula weight | 13243.14 |
| Authors | Vilanova, M.,Callis, M.,Laurents, D.V.,Ribo, M.,Bruix, M.,Serrano, S. (deposition date: 2012-05-14, release date: 2012-10-24, Last modification date: 2023-06-14) |
| Primary citation | (1)H, (13)C and (15)N resonance assignments of the Onconase FL-G zymogen. Biomol.Nmr Assign., 2012 Cited by PubMed 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. PubMed: 22392335DOI: 10.1007/s12104-012-9367-0 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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