Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site(585 views) Oliva R, Falcigno L, D'Auria G, Dettin M, Scarinci C, Pasquato A, Di Bello C, Paolillo L
Keywords: Amino Acid Sequence, Catalytic Domain, Circular Dichroism, Consensus Sequence, Furin, Hiv Envelope Protein Gp160 Chemistry Metabolism, Hiv Infections Metabolism Virology, Hiv-1 Chemistry, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments Chemistry, Protein Conformation, Sequence Homology, Subtilisins Chemistry Metabolism, Conformation Analysis, Molecular Modeling, Nmr Spectroscopy, Glycoprotein Gp 160, Virus Glycoprotein, Article, Enzyme Activity, Human Immunodeficiency Virus, Nonhuman, Nuclear Magnetic Resonance Spectroscopy, Priority Journal, Protein Degradation, Protein Structure, Virus Envelope,
Affiliations: *** IBB - CNR ***
Dipartimento di Chimica, Universita di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cintia, 80126 Napoli, Italy.
Ist. Biostrutture/Bioimmagini C.N.R., Universita di Napoli Federico II, Via Mezzocannone 4, 80134 Napoli, Italy
Dipto. Proc. Chimici dell'Ingegneria, Università di Padova, Via Marzolo 9, 35131 Padova, Italy
References: Not available.
Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site
The selective proteolytic activation of the HIV-1 envelope glycoprotein gp160 by furin and other precursor convertases (PCs) occurs at the carboxyl side of the sequence Arg508-Glu-Lys-Arg511 (site 1), in spite of the presence of another consensus sequence: Lys500-Ala-Lys-Arg503 (site 2). We report on the solution structural analysis of a 19-residue synthetic peptide, p498. which spans the two gp160-processing sites 1 and 2, and is properly digested by furin at site 1. A molecular model is obtained for p498, by means of molecular dynamics simulations, from NMR data collected in trifluoroethanol/water. The peptide N-terminal side presents a 9-residue helical segment, enclosing the processing site 2; the C-terminal segment can be described as a loop exposing the processing site 1. A hypothesis for the docking of p498 onto the catalytic domain of human furin, modeled by homology and fitting previous site-directed mutagenesis studies, is also presented. p498 site 1 is shown to have easy access to the furin catalytic site, unlike the nonphysiological site 2. Finally, on the basis of available data. we suggest a possible structural motif required for the gp160-PCs recognition.
Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site
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