NMR structural determination of viscotoxin A3 from Viscum album L. (Articolo in rivista)

Type
Label
  • NMR structural determination of viscotoxin A3 from Viscum album L. (Articolo in rivista) (literal)
Anno
  • 2000-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1042/0264-6021:3500569 (literal)
Alternative label
  • Romagnoli, S and Ugolini, R and Fogolari, F and Schaller, G and Urech, K and Giannattasio, M and Ragona, L and Molinari, H (2000)
    NMR structural determination of viscotoxin A3 from Viscum album L.
    in Biochemical journal (Lond., 1984)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Romagnoli, S and Ugolini, R and Fogolari, F and Schaller, G and Urech, K and Giannattasio, M and Ragona, L and Molinari, H (literal)
Pagina inizio
  • 569 (literal)
Pagina fine
  • 577 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 350 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Molinari, H (Reprint Author), Dipartimento Sci & Tecnol, Ca Vignal 1,Strada Grazie, I-37134 Verona, Italy. Dipartimento Sci & Tecnol, I-37134 Verona, Italy. Hischia Inst, Verein Krebsforsch, CH-4144 Arlesheim, Switzerland. Univ Naples, Fac Agr, Dipartimento Arboricoltura Bot & Patol Vegetale, I-80100 Naples, Italy. Ist Chim Macromol, Lab NMR, I-20131 Milan, Italy. (literal)
Titolo
  • NMR structural determination of viscotoxin A3 from Viscum album L. (literal)
Abstract
  • The high-resolution three-dimensional structure of the plant toxin viscotoxin A3, from Viscum album L., has been determined in solution by H-1 NMR spectroscopy at pH 3.6 and 12 degrees C (the structure has been deposited in the Protein Data Bank under the id. code 1EDO). Experimentally derived restraints including 734 interproton distances from nuclear Overhauser effect measurements, 22 hydrogen bonds, 32 phi angle restraints from J coupling measurements, together with three disulphide bridge constraints were used as input in restrained molecular dynamics, followed by minimization, using DYANA and Discover. Backbone and heavy atom root-mean-square deviations were 0.47+/-0.11 Angstrom (1 Angstrom = 10(-10) m) and 0.85+/-0.13 Angstrom respectively. Viscotoxin A3 consists of two alpha-helices connected by a turn and a short stretch of antiparallel beta-sheet. This fold is similar to that found in other thionins, such as crambin, hordothionin-alpha and -beta, phoratoxin A and purothionin-alpha, and -beta. The difference in the observed biological activity for thionins of known structure is discussed in terms of the differences in the calculated surface potential distribution, playing an important role in their function through disruption of cell membranes. In addition, the possible role in DNA binding of the helix-turn-helix motif of viscotoxin A3 is discussed. (literal)
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