Onconase (ONC), a member of the RNase A superfamily, is an effective cancer killer. It is currently used in treatment of various forms of cancer. ONC antitumor properties depend on its ribonucleolytic activity that is low in comparison with other members of the superfamily.The structural and dynamic changes induced by specific mutations were correlated with modifications in the activity and thermal stability of the mutants. Furthermore, our results provide the molecular bases to explain the lower catalytic activity of ONC compared to RNase A.
CRYSTAL STRUCTURES AND MOLECULAR DYNAMIC STUDIES OF ONCONASE MUTANTS / Merlino, Antonello; Sica, Filomena; Mazzarella, Lelio; A., Carannante; A., DI FIORE; DI DONATO, Alberto; Notomista, Eugenio. - (2005), pp. 12-12. (Intervento presentato al convegno 7th International meeting on ribonucleases tenutosi a Stara Lesna, Slovak republic nel June 16-20, 2005).
CRYSTAL STRUCTURES AND MOLECULAR DYNAMIC STUDIES OF ONCONASE MUTANTS
MERLINO, ANTONELLO;SICA, FILOMENA;MAZZARELLA, LELIO;DI DONATO, ALBERTO;NOTOMISTA, EUGENIO
2005
Abstract
Onconase (ONC), a member of the RNase A superfamily, is an effective cancer killer. It is currently used in treatment of various forms of cancer. ONC antitumor properties depend on its ribonucleolytic activity that is low in comparison with other members of the superfamily.The structural and dynamic changes induced by specific mutations were correlated with modifications in the activity and thermal stability of the mutants. Furthermore, our results provide the molecular bases to explain the lower catalytic activity of ONC compared to RNase A.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
