he role of the hinge loop in domain-swapping: The special case of Bovine seminal Ribonuclease. (Articolo in rivista)

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Label
  • he role of the hinge loop in domain-swapping: The special case of Bovine seminal Ribonuclease. (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Alternative label
  • Picone, D., Di Fiore, A., Ercole, C., Franzese, M., Sica, F., Tomaselli, S., Mazzarella, L (2005)
    he role of the hinge loop in domain-swapping: The special case of Bovine seminal Ribonuclease.
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Picone, D., Di Fiore, A., Ercole, C., Franzese, M., Sica, F., Tomaselli, S., Mazzarella, L (literal)
Pagina inizio
  • 13771 (literal)
Pagina fine
  • 13778 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 280 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • Pubblicazione su rivista scientifica (literal)
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • he role of the hinge loop in domain-swapping: The special case of Bovine seminal Ribonuclease. (literal)
Abstract
  • Bovine seminal RNase (BS-RNase) is a covalent homodimeric enzyme homologous to pancreatic RNase (RNase A), endowed with a no. of special biol. functions. It is isolated as an equil. mixt. of swapped (MxM) and unswapped (M=M) dimers. The interchanged N termini are hinged on the main bodies through the peptide 16-22, which changes conformation in the two isomers. At variance with other proteins, domain swapping in BS-RNase involves two dimers having a similar and highly constrained quaternary assocn., mainly dictated by two interchain disulfide bonds. This provides the opportunity to study the intrinsic ability to swap as a function of the hinge sequence, without addnl. effects arising from dissocn. or quaternary structure modifications. Two variants, having Pro19 or the whole sequence of the hinge replaced by the corresponding residues of RNase A, show equil. and kinetic parameters of the swapping similar to those of the parent protein. In comparison, the x-ray structures of MxM indicate, within a substantial constancy of the quaternary assocn., a greater mobility of the hinge residues. The relative insensitivity of the swapping tendency to the substitutions in the hinge region, and in particular to the replacement of Pro19 by Ala, contrasts with the results obtained for other swapped proteins and can be rationalized in terms of the unique features of the seminal enzyme. Moreover, the results indirectly lend credit to the hypothesis that the major role of Pro19 resides in directing the assembly of the non-covalent dimer, the species produced by selective redn. of the interchain disulfides and considered responsible for the special biol. functions of BS-RNase. (literal)
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