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NMR structure of a biologically active peptide containing the RNA-binding domain of human immunodeficiency virus type 1 Tat.

The Tat protein of human immunodeficiency virus type 1 enhances transcription by binding to a specific RNA element on nascent viral transcripts. Binding is mediated by a 10-amino acid basic domain that is rich in arginines and lysines. Here we report the three-dimensional peptide backbone structure...

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Main Authors: Mujeeb, A, Bishop, K, Peterlin, B M, Turck, C, Parslow, T G, James, T L, Rhoads, D M, Kaspi, C I, Levings, C S, Siedow, J N, Harata, M, Karwan, A, Wintersberger, U, Larue, L, Ohsugi, M, Hirchenhain, J, Kemler, R, Civardi, L, Xia, Y, Edwards, K J, Schnable, P S, Nikolau, B J, Maruyama, I N, Maruyama, H I, Brenner, S, Tetaud, E, Bringaud, F, Chabas, S, Barrett, M P, Baltz, T, Ishaq, M, Stoner, G L, Schmidt, K F, Kruse, M, Hatt, H, Borchelt, D R, Lee, M K, Slunt, H S, Guarnieri, M, Xu, Z S, Wong, P C, Brown, R H, Price, D L, Sisodia, S S, Cleveland, D W, Meador-Woodruff, J H, Damask, S P, Watson, S J, Huber, B E, Austin, E A, Richards, C A, Davis, S T, Good, S S, Tinsley, J M, Blake, D J, Zuellig, R A, Davies, K E, Brighty, D W, Rosenberg, M, Smiley, J A, Benkovic, S J, Whitesell, L, Mimnaugh, E G, De Costa, B, Myers, C E, Neckers, L M, Wang, X M, Yew, N, Peloquin, J G, Vande Woude, G F, Borisy, G G, Trounce, I, Neill, S, Wallace, D C, Purves, D, White, L E, Pan, Z Q, Amin, A A, Gibbs, E, Niu, H, Hurwitz, J, Carayannopoulos, L, Max, E E, Capra, J D, Fontan, E, Briend, E, Saklani-Jusforgues, H, d'Alayer, J, Vandekerckhove, J, Fauve, R M, Dixon, J F, Los, G V, Hokin, L E, Schmidt-Ott, U, González-Gaitán, M, Jäckle, H, Technau, G M, Schwarzman, A L, Gregori, L, Vitek, M P, Lyubski, S, Strittmatter, W J, Enghilde, J J, Bhasin, R, Silverman, J, Weisgraber, K H, Coyle, P K, Shang, Z, Isaac, V E, Li, H, Patel, L, Catron, K M, Curran, T, Montelione, G T, Abate, C, Näslund, J, Schierhorn, A, Hellman, U, Lannfelt, L, Roses, A D, Tjernberg, L O, Silberring, J, Gandy, S E, Winblad, B, Greengard, P, Liu, H, Wang, H, Sheng, M, Jan, L Y, Jan, Y N, Basbaum, A I, Ina, Y, Gojobori, T, Schena, M, Davis, R W, Lu, S J, Rowan, S, Bani, M R, Ben-David, Y, Bianchi, V, Borella, S, Calderazzo, F, Ferraro, P, Chieco Bianchi, L, Reichard, P, Gu, Q, Liu, Y, Cynader, M S, Joseph, P, Jaiswal, A K, Atkinson, E M, Palcic, M M, Hindsgaul, O, Long, S R, Satoh, T, Satoh, H, Iwahara, S, Hrkal, Z, Peyton, D H, Muller-Eberhard, U, Ruchaud, S, Duprez, E, Gendron, M C, Houge, G, Genieser, H G, Jastorff, B, Doskeland, S O, Lanotte, M, Ahner, B A, Price, N M, Morel, F M, Du, Y, Maslov, D A, Chang, K P, France, L L, Piatti, P G, Newman, J F, Toth, I, Gibbons, W A, Brown, F, Zhang, D, Botos, I, Gomis-Rüth, F X, Doll, R, Blood, C, Njoroge, F G, Fox, J W, Bode, W, Meyer, E F, Glerum, D M, Tzagoloff, A, Friedman, E, Bale, A E, Carson, E, Boson, W L, Nordenskjöld, M, Ritzén, M, Ferreira, P C, Jammal, A, De Marco, L, Kappler, J, White, J, Kozono, H, Clements, J, Marrack, P, de Koning, E J, Morris, E R, Hofhuis, F M, Posthuma, G, Höppener, J W, Morris, J F, Capel, P J, Clark, A, Verbeek, J S, Schrével, J, Sinou, V, Grellier, P, Frappier, F, Guénard, D, Potier, P, Packard, M G, Cahill, L, McGaugh, J L, Purpura, K P, Victor, J D, Katz, E, Probst, W C, Cropper, E C, Heierhorst, J, Hooper, S L, Jaffe, H, Vilim, F, Beushausen, S, Kupfermann, I, Weiss, K R, Hofmann, G E, Hand, S C
Formato: Artigo
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Publicado em: 1994
Assuntos:
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Descrição
Resumo:The Tat protein of human immunodeficiency virus type 1 enhances transcription by binding to a specific RNA element on nascent viral transcripts. Binding is mediated by a 10-amino acid basic domain that is rich in arginines and lysines. Here we report the three-dimensional peptide backbone structure of a biologically active 25-mer peptide that contains the human immunodeficiency virus type 1 Tat basic domain linked to the core regulatory domain of another lentiviral Tat--i.e., that from equine infectious anemia virus. Circular dichroism and two-dimensional proton NMR studies of this hybrid peptide indicate that the Tat basic domain forms a stable alpha-helix, whereas the adjacent regulatory sequence is mostly in extended form. These findings suggest that the tendency to form stable alpha-helices may be a common property of arginine- and lysine-rich RNA-binding domains.