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)
Pagina inizio
  • 689 (literal)
Pagina fine
  • 695 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 73 (literal)
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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