3hg6
Crystal Structure of the Recombinant Onconase from Rana pipiensCrystal Structure of the Recombinant Onconase from Rana pipiens
Structural highlights
FunctionRNP30_LITPI Basic protein with antiproliferative/cytotoxic activity against several tumor cell lines in vitro, as well as antitumor in vivo. It exhibits a ribonuclease-like activity against high molecular weight ribosomal RNA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedOnconase 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 degrees below the global unfolding temperature, reaching a maximum population of nearly 60%, 10 degrees below the global unfolding temperature. Three-state thermal unfolding of onconase.,Casares-Atienza S, Weininger U, Camara-Artigas A, Balbach J, Garcia-Mira MM Biophys Chem. 2011 Dec;159(2-3):267-74. doi: 10.1016/j.bpc.2011.07.005. Epub 2011 , Jul 24. PMID:21840114[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||