3HG6
Crystal Structure of the Recombinant Onconase from Rana pipiens
Summary for 3HG6
| Entry DOI | 10.2210/pdb3hg6/pdb |
| Descriptor | Onconase, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | alpha and beta protein, endonuclease, hydrolase, nuclease |
| Biological source | Rana pipiens |
| Total number of polymer chains | 1 |
| Total formula weight | 12321.99 |
| Authors | Camara-Artigas, A.,Gavira, J.A.,Casares-Atienza, S.,Weininger, U.,Balbach, J.,Garcia-Mira, M.M. (deposition date: 2009-05-13, release date: 2010-05-19, Last modification date: 2024-11-06) |
| Primary citation | Casares-Atienza, S.,Weininger, U.,Camara-Artigas, A.,Balbach, J.,Garcia-Mira, M.M. Three-state thermal unfolding of onconase. Biophys.Chem., 159:267-274, 2011 Cited by PubMed Abstract: Onconase is a member of the ribonuclease A superfamily currently in phase IIIb clinical trials as a treatment for malign mesothelioma due to its cytotoxic activity selective against tumor-cells. In this work, we have studied the equilibrium thermal unfolding of onconase using a combination of several structural and biophysical techniques. Our results indicate that at least one significantly populated intermediate, which implies the exposure of hydrophobic surface and significant changes in the environment around Trp3, occurs during the equilibrium unfolding process of this protein. The intermediate begins to populate at about 30° below the global unfolding temperature, reaching a maximum population of nearly 60%, 10° below the global unfolding temperature. PubMed: 21840114DOI: 10.1016/j.bpc.2011.07.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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