Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site, 2: Relevance of an N-terminal helix. (Articolo in rivista)

Type
Label
  • Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site, 2: Relevance of an N-terminal helix. (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Oliva, Romina; Falcigno, Lucia; D'Auria, Gabriella; Dettin, Monica; Scarinci, Claudia; Pasquato, Antonella; Di Bello, Carlo; Paolillo, Livio. (2003)
    Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site, 2: Relevance of an N-terminal helix.
    in ChemBioChem (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Oliva, Romina; Falcigno, Lucia; D'Auria, Gabriella; Dettin, Monica; Scarinci, Claudia; Pasquato, Antonella; Di Bello, Carlo; Paolillo, Livio. (literal)
Pagina inizio
  • 727 (literal)
Pagina fine
  • 733 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 4 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site, 2: Relevance of an N-terminal helix. (literal)
Abstract
  • Proteolytic activation of the HIV-1 envelope glycoprotein gp160 is selectively performed by the proprotein convertase furin at the C-terminus of the sequence R508-E-K-R511 (site 1), in spite of the presence of another consensus sequence, Lys500-Ala-Lys-Arg503 (site 2). On the basis of the soln. structural anal. of the synthetic peptide P498, spanning the gp160 sequence Pro498-Gly516, we previously suggested a possible role of an N-terminal helix in regulating the exposure and accessibility of the gp160 physiol. cleavage site, enclosed in a loop. Here we report on the activity and conformation of the 23-residue peptide h-REKR, designed to exhibit a large N-terminal helix, followed by the gp160 native sequence, Arg508-Gly516. H-REKR is digested by furin with high efficiency, comparable to the full native p498. CD analyses, in mixts. from pure water to 98% trifluoroethanol, outline a significant content of helical structure in the peptide conformation. The mol. model obtained from NMR data collected in trifluoroethanol/water, by means of DYANA and AMBER simulations, indeed has helical structure on a large N-terminal segment. Such a long helix does not seem to affect the loop conformation of the C-terminal site 1-contg. sequence, which exhibits the same proton chem. shifts already obsd. for the full native p498. (literal)
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