http://www.cnr.it/ontology/cnr/individuo/prodotto/ID13455
Population shift vs induced fit: the case of bovine seminal ribonuclease swapping dimer. (Articolo in rivista)
- Type
- Label
- Population shift vs induced fit: the case of bovine seminal ribonuclease swapping dimer. (Articolo in rivista) (literal)
- Anno
- 2004-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/bip.20016 (literal)
- Alternative label
Merlino, Antonello; Vitagliano, Luigi; Sica, Filomena; Zagari, Adriana; Mazzarella, Lelio. (2004)
Population shift vs induced fit: the case of bovine seminal ribonuclease swapping dimer.
in Biopolymers (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Merlino, Antonello; Vitagliano, Luigi; Sica, Filomena; Zagari, Adriana; Mazzarella, Lelio. (literal)
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- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Dipartimento di Chimica,
Universita` degli Studi di
Napoli \"Federico II,\"
Via Cynthia,
80126 Napoli,
Italy
2 Dipartimento di Scienze
Farmaceutiche,
Universita` di Salerno,
Via ponte don Melillo,
84084,
Fisciano (Sa),
Italy
3 Istituto di Biostrutture e
Bioimmagini,
CNR,
Via Mezzocannone 6,
80134 Napoli,
Italy (literal)
- Titolo
- Population shift vs induced fit: the case of bovine seminal ribonuclease swapping dimer. (literal)
- Abstract
- Bovine seminal RNase (BS-RNase) is a unique member of the pancreatic-like RNase superfamily. This enzyme exists as two conformational isomers with distinctive biol. properties. The structure of the major isomer is characterized by the swapping of the N-terminal segment (M´M BS-RNase). In this article, the crystal structures of the ligand-free M´M BS-RNase and its complex with 2'-deoxycitidylyl(3',5')-2'-deoxyadenosine derived from isomorphous crystals have been refined. Interestingly, the comparison between this novel ligand-free form and the previously published sulfate-bound structure reveals significant differences. In particular, the ligand-free M´M BS-RNase is closer to the structure of M´M BS-RNase productive complexes than to the sulfate-bound form. These results reveal that M´M BS-RNase presents a remarkable flexibility, despite the structural constraints of the interchain disulfide bridges and the swapping of the N-terminal helixes. These findings have important implications to the ligand binding mechanism of M´M BS-RNase. Indeed, a population shift rather than a substrate-induced conformational transition may occur in the M´M BS-RNase ligand binding process. (literal)
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