The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase. (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Alternative label

• Merlino, A., Mazzarella, L., Di Fiore, A., Carannante, A., Notomista, E., Di Donato, A., Sica, F. (2005)
  The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase.
  
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Merlino, A., Mazzarella, L., Di Fiore, A., Carannante, A., Notomista, E., Di Donato, A., Sica, F. (literal)

Pagina inizio

• 17953 (literal)

Pagina fine

• 17980 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 280 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto

• Pubblicazione scientifica (literal)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase. (literal)

Abstract

• Onconase (ONC), a member of the RNase A superfamily extd. from oocytes of Rana pipiens, 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 most damaging side effect from Onconase treatment is renal toxicity, which seems to be caused by the unusual stability of the enzyme. Therefore, mutants with reduced thermal stability and/or increased catalytic activity may have significant implications for human cancer chemotherapy. In this context, we have detd. the crystal structures of two Onconase mutants (M23L-ONC and C87S,des103-104-ONC) and performed mol. dynamic simulations of ONC and C87S,des103-104-ONC with the aim of explaining on structural grounds the modifications of the activity and thermal stability of the mutants. The results also provide the mol. bases to explain the lower catalytic activity of Onconase compared with RNase A and the unusually high thermal stability of the amphibian enzyme. (literal)

Prodotto di

• Determinazione della struttura tridimensionale di biomolecole complesse con tecniche spettroscopiche e cristallografiche (PM.P01.022.001) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• Lelio Mazzarella (Unità di personale esterno)

Insieme di parole chiave

• Keywords of "The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase." (Insieme di parole chiave)

Incoming links:

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Determinazione della struttura tridimensionale di biomolecole complesse con tecniche spettroscopiche e cristallografiche (PM.P01.022.001) (Modulo)

Autore CNR di

• Lelio Mazzarella (Unità di personale esterno)

Insieme di parole chiave di

• Keywords of "The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase." (Insieme di parole chiave)