Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site 3: Role of site-specific mutations(589 views) Falcigno L, Oliva R, D'Auria G, Maletta M, Dettin M, Pasquato A, Di Bello C, Paolillo L
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2004 Dec 3; 5(12): 1653-1661.
Keywords: Catalytic Domain, Furin Pharmacology, Hiv Envelope Protein Gp160 Chemistry Metabolism, Hiv-1 Chemistry, Humans, Mutagenesis, Site-Directed, Peptide Fragments Chemistry, Point Mutation, Proline Chemistry, Protein Conformation Drug Effects, Conformation Analysis, D-Amino Acids, Nmr Spectroscopy, Dextro Amino Acid, Glycoprotein Gp 160, Proprotein Convertase, Proteinase, Unclassified Drug, Amino Acid Sequence, Amino Terminal Sequence, Article, Enzyme Activity, Human Immunodeficiency Virus 1, Molecular Recognition, Nonhuman, Nuclear Magnetic Resonance Spectroscopy, Priority Journal, Protein Degradation, Protein Structure, Sequence Analysis, Site Directed Mutagenesis, Structure Activity Relation, Virus Envelope, Virus Infectivity,
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 6, 80134 Napoli, Italy
Dipto. Proc. Chimici Ingegneria, Università di Padova, Via Marzolo 9, 35131 Padova, Italy
References: Not available.
Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site 3: Role of site-specific mutations
Proteolytic processing of HIV gp 160 to produce gp 120 and gp41 is performed by PC enzymes. This process is a prerequisite for the virus infectivity, since both gp120 and gp41 participate in the virus HIV-1 entry mechanism. The structure of the gp120/gp47 junction remains to be elucidated, and the structural features required for molecular recognition between HIV-1 gp160 and proteolytic enzymes have not been clarified. Furin is the best PC candidate for the gp 160 proteolytic processing known to date. In previous studies on model peptides, we hove shown the relevance of an N-terminal helix for the proper recognition of the gp160 processing site by furin. Here we analyze the effect of point mutations in peptides locking a regular N-terminal helix. To this end, we present the structure-activity characterization of three peptide analogues of the HIV gp 160 processing site that all present mutations in proline at positions P3 and/or P2', while sharing the some N-terminal sequence, containing helix-breaking D-amino acids. Conformational analysis of the peptides was carried out in solution by NMR techniques, and furin's efficiency in cleaving them was measured. Structural findings are presented and discussed in relation to the different exhibited activity.
Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site 3: Role of site-specific mutations
Kim YH, Shin SW, Pellicano R, Fagoonee S, Choi IJ, Kim YI, Park B, Choi JM, Kim SG, Choi J, Park JY, Oh S, Yang HJ, Lim JH, Im JP, Kim JS, Jung HC, Ponzetto A, Figura N, Malfertheiner P, Choi IJ, Kook MC, Kim YI, Cho SJ, Lee JY, Kim CG, Park B, Nam BH, Bae SE, Choi KD, Choe J, Kim SO, Na HK, Choi JY, Ahn JY, Jung KW, Lee J, Kim DH, Chang HS, Song HJ, Lee GH, Jung HY, Seta T, Takahashi Y, Noguchi Y, Shikata S, Sakai T, Sakai K, Yamashita Y, Nakayama T, Leja M, Park JY, Murillo R, Liepniece-karele I, Isajevs S, Kikuste I, Rudzite D, Krike P, Parshutin S, Polaka I, Kirsners A, Santare D, Folkmanis V, Daugule I, Plummer M, Herrero R, Tsukamoto T, Nakagawa M, Kiriyama Y, Toyoda T, Cao X, Corral JE, Mera R, Dye CW, Morgan DR, Lee YC, Lin JT, Garcia Martin R, Matia Cubillo A, Lee SH, Park JM, Han YM, Ko WJ, Hahm KB, Leontiadis GI, Ford AC, Ichinose M, Sugano K, Jeong M, Park JM, Han YM, Park KY, Lee DH, Yoo JH, Cho JY, Hahm KB, Bang CS, Baik GH, Shin IS, Kim JB, Suk KT, Yoon JH, Kim YS, Kim DJ * Helicobacter pylori Eradication for Prevention of Metachronous Recurrence after Endoscopic Resection of Early Gastric Cancer(682 views) N Engl J Med (ISSN: 0028-4793, 0028-4793linking, 1533-4406electronic), 2015 Jun; 30642104201566393291: 749-756. Impact Factor:59.558 ViewExport to BibTeXExport to EndNote