Role of Flexibility in Protein-DNA-Drug Recognition: The Case of Asp677Gly-Val703Ile Topoisomerase Mutant Hypersensitive to Camptothecin. (Articolo in rivista)

Type

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

Label

• Role of Flexibility in Protein-DNA-Drug Recognition: The Case of Asp677Gly-Val703Ile Topoisomerase Mutant Hypersensitive to Camptothecin. (Articolo in rivista) (literal)

Anno

• 2012-01-01T00:00:00+01:00 (literal)

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

• 10.1155/2012/206083 (literal)

Alternative label

• D'Annessa, Ilda; Tesauro, Cinzia; Fiorani, Paola; Chillemi, Giovanni; Castelli, Silvia; Vassallo, Oscar; Capranico, Giovanni; Desideri, Alessandro (2012)
  Role of Flexibility in Protein-DNA-Drug Recognition: The Case of Asp677Gly-Val703Ile Topoisomerase Mutant Hypersensitive to Camptothecin.
  in Journal of amino acids
  (literal)

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

• D'Annessa, Ilda; Tesauro, Cinzia; Fiorani, Paola; Chillemi, Giovanni; Castelli, Silvia; Vassallo, Oscar; Capranico, Giovanni; Desideri, Alessandro (literal)

Pagina inizio

• 206083 (literal)

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

• 2012 (literal)

Rivista

• Journal of amino acids (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• National Research Council (CNR) and Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica, Rome 00133, Italy. (literal)

Titolo

• Role of Flexibility in Protein-DNA-Drug Recognition: The Case of Asp677Gly-Val703Ile Topoisomerase Mutant Hypersensitive to Camptothecin. (literal)

Abstract

• Topoisomerases I are ubiquitous enzymes that control DNA topology within the cell. They are the unique target of the antitumor drug camptothecin that selectively recognizes the DNA-topoisomerase covalent complex and reversibly stabilizes it. The biochemical and structural-dynamical properties of the Asp677Gly-Val703Ile double mutant with enhanced CPT sensitivity have been investigated. The mutant displays a lower religation rate of the DNA substrate when compared to the wild-type protein. Analyses of the structural dynamical properties by molecular dynamics simulation show that the mutant has reduced flexibility and an active site partially destructured at the level of the Lys532 residue. These results demonstrate long-range communication mechanism where reduction of the linker flexibility alters the active site geometry with the consequent lowering of the religation rate and increase in drug sensitivity. (literal)

Prodotto di

• Target molecolari, modelli preclinici ed immunoterapia in Oncologia (ME.P03.015.001) (Modulo)

Autore CNR

• PAOLA FIORANI (Unità di personale interno)

Incoming links:

Prodotto

• Target molecolari, modelli preclinici ed immunoterapia in Oncologia (ME.P03.015.001) (Modulo)

Autore CNR di

• PAOLA FIORANI (Unità di personale interno)

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

• Journal of amino acids (Rivista)