Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site(479 views) Oliva R, Leone M, Falcigno L, D'Auria G, Dettin M, Scarinci C, Di Bello C, Paolillo L
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2002 Mar 15; 8(6): 1467-1473.
Keywords: Conformation Analysis, Hiv, Molecular Modeling Proteases, Protein Structures, Molecular Dynamics, Mutagenesis, Nuclear Magnetic Resonance, Catalytic Sites, Furin, Glycoprotein Gp 160, Trifluoroethanol, Water, Alpha Helix, Amino Acid Sequence, Amino Terminal Sequence, Article, Carboxy Terminal Sequence, Consensus Sequence, Enzyme Active Site, Human Immunodeficiency Virus 1, Molecular Recognition, Nuclear Magnetic Resonance Spectroscopy, Protein Degradation, Protein Domain, Protein Motif, Protein Tertiary Structure, Sequence Homology, Site Directed Mutagenesis, Structure Analysis, Catalytic Domain, Hiv Envelope Protein Gp160, Peptide Fragments, Secondary, Solutions, Subtilisins, Hiv Envelope Protein Gp160 Chemistry Metabolism, Peptide Fragments Chemistry, Subtilisins Chemistry Metabolism,
Affiliations: *** IBB - CNR ***
Dipartimento di Chimica, Università di Napoli Federico II, Complesso Universitario Monte S. Angelo, via Cintia, 80126 Napoli, Italy
Centro di Studio di Biocristallografia, C.N.R., Università di Napoli Federico II, Via Mezzocannone 4, 80134 Napoli, Italy
Dipartimento di Processi Chimici dell'Ingegneria, Università di Padova, Via Marzolo 9, 35131 Padova, Italy
References: Stein, B.S., Engleman, E.G., (1990) J. Biol. Chem., 265, pp. 2640-264
Weber, J.N., Weiss, R.A., (1988) Sci. Am., 259, pp. 100-109
Hallenberger, S., Bosh, V., Angliker, H., Shaw, E., Klenk, H.D., Garten, W., (1992) Nature, 360, pp. 358-361
Decroly, E., Vandenbranden, M., Ruysschaert, J.M., Cogniaux, J., Jacob, G.S., Howard, S.C., Marshall, G., Seidah, N.G., (1994) J. Biol. Chem., 269, pp. 12240-12247
Moulard, M., Decroly, E., (2000) Biochim. Biophys. Acta, 1469, pp. 121-132. , and references therein
McCune, J.M., Rabin, L.B., Feinberg, M.B., Lieberman, M., Kosek, J.C., Reyes, G.R., Weissman, I.L., (1988) Cell, 53, pp. 55-67
Freed, E.O., Myers, D.J., Risser, R., (1989) J. Virol., 63, pp. 4670-4675
Guo, H.G., Veronese, F.D., Tschachler, E., Pal, R., Kalyanaraman, V.S., Gallo, R.C., Reitz Jr., M.S., (1990) Virology, 174, pp. 217-224
Bosch, V., Pawlita, M., (1990) J. Virol., pp. 2337-2344
Turner, G., Summers, M.F., (1999) J. Mol. Biol., 285, pp. 1-32
Brakch, N., Dettin, M., Scarinci, C., Seidah, N.G., Di Bello, C., (1995) Biochem. Biophys. Res. Commun., 213, pp. 356-361
Decroly, E., Wouters, S., Di Bello, C., Lazure, C., Ruysschaert, J.M., Seidah, N.G., (1996) J. Biol. Chem., 271, pp. 30442-30450
Moulard, M., Challoin, L., Canarelli, S., Mabrouk, K., Darbon, H., (1998) Biochemistry, 37, pp. 4510-4517
Siezen, R.J., Creemers, J.W., Van De Ven, W.J., (1994) Eur. J. Biochem., 222, pp. 255-266. , and references therein
Creemers, J.W., Siezen, R.J., Roebroek, A.J.M., Ayoubi, T.A.Y., Huylebroeck, D., Van De Ven, W.J.M., (1993) J. Biol. Chem., 268, pp. 21826-21834
Wishart, D.S., Sykes, B.D., Richards, F.M., (1991) J. Mol. Biol., 222, pp. 311-333
Güntert, P., Mumenthaler, C., Wüthrich, K., (1997) J. Mol. Biol., 273, pp. 283-298
Güntert, P., Wüthrich, K., (1991) J. Biomol. NMR, 1, pp. 447-456
McLachlan, A.D., (1979) J. Mol. Biol., 128, pp. 49-79
Gros, P., Betzel, C., Dauter, Z., Wilson, K.S., Hol, W.G., (1989) J. Mol. Biol., 210, pp. 347-367
Siezen, R.J., De Vos, W.M., Dijkstra, B.W., (1991) Prot. Eng., 4, pp. 719-737
Schechter, I., Berger, A., (1967) Biochem. Biophys. Res. Commun., 27, pp. 157-162
Segawa, S., Fukuno, T., Fujiwara, K., Noda, Y., (1991) Biopolymers, 31, pp. 497-509
Jimenez, M.A., Bruix, M., Gonzales, C., Blanco, F.J., Nieto, J.L., Herranz, J., Rico, M., (1993) Eur. J. Biochem., 211, pp. 569-581
Brooks III, C.L., Karplus, M., Pettitt, B.M., Proteins: A theoretical perspective of dynamics, structure and thermodynamics (1988) Advances in Chemical Physics, 71. , Wiley, New York
McCammon, J.A., Wolynes, P.G., Karplus, M., (1979) Biochemistry, 18, pp. 927-942
Melacini, G., Zhu, Q., Goodman, M., (1997) Biochemistry, 36, pp. 1233-1241
Hockney, R.W., (1970) Methods in Computational Physics. Vol. 9 (Plasma Physics), 9, pp. 136-211. , Academic Press, New York, London
Van Gunsteren, W.F., Berendsen, H.J.C., (1990) Angew. Chem., 101, pp. 1020-1051
(1990) Angew. Chem. Int. Ed. Engl., 29, pp. 992-1023
Wüthrich, K., Billeter, M., Brown, W., (1983) J. Mol. Biol., 169, pp. 949-961
Koradi, R., Billeter, M., Wüthrich, K., (1996) J. Mol. Graphics, 14, pp. 51-55
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
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(295 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