Thrombin-aptamer recognition: a revealed ambiguity (Articolo in rivista)

Type

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

Label

• Thrombin-aptamer recognition: a revealed ambiguity (Articolo in rivista) (literal)

Anno

• 2011-01-01T00:00:00+01:00 (literal)

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

• 10.1093/nar/gkr522 (literal)

Alternative label

• Russo Krauss I, Merlino A, Giancola C, Randazzo A, Mazzarella L, Sica F (2011)
  Thrombin-aptamer recognition: a revealed ambiguity
  in Nucleic acids research
  (literal)

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

• Russo Krauss I, Merlino A, Giancola C, Randazzo A, Mazzarella L, Sica F (literal)

Pagina inizio

• 7858 (literal)

Pagina fine

• 7867 (literal)

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

• 39 (literal)

Rivista

• Nucleic acids research (Rivista)

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

• 10 (literal)

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

• 17 (literal)

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

• Università di Napoli Federico II, Via Cintia, Napoli, Italia Istituto di Biostrutture e Bioimmagini - CNR, NAPOLI (literal)

Titolo

• Thrombin-aptamer recognition: a revealed ambiguity (literal)

Abstract

• Aptamers are structured oligonucleotides that recognize molecular targets and can function as direct protein inhibitors. The best-known example is the thrombin-binding aptamer, TBA, a single-stranded 15-mer DNA that inhibits the activity of thrombin, the key enzyme of coagulation cascade. TBA folds as a G-quadruplex structure, as proved by its NMR structure. The X-ray structure of the complex between TBA and human ?-thrombin was solved at 2.9-Å resolution, but did not provide details of the aptamer conformation and the interactions with the protein molecule. TBA is rapidly processed by nucleases. To improve the properties of TBA, a number of modified analogs have been produced. In particular, a modified TBA containing a 5'-5' polarity inversion site, mTBA, has higher stability and higher affinity toward thrombin with respect to TBA, although it has a lower inhibitory activity. We present the crystal structure of the thrombin-mTBA complex at 2.15-Å resolution; the resulting model eventually provides a clear picture of thrombin-aptamers interaction, and also highlights the structural bases of the different properties of TBA and mTBA. Our findings open the way for a rational design of modified aptamers with improved potency as anticoagulant drugs. (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

• Antonello Merlino (Unità di personale esterno)
• Filomena Sica (Unità di personale esterno)
• Lelio Mazzarella (Persona)

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

• Filomena Sica (Unità di personale esterno)
• Antonello Merlino (Unità di personale esterno)
• Lelio Mazzarella (Persona)

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

• Nucleic acids research (Rivista)