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Volumn 245, Issue 3, 1997, Pages 581-588

Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution

Author keywords

CD4; human immunodeficiency virus 1 Vpts; lysin; NMR; solution structure

Indexed keywords

CD4 ANTIGEN; LYMPHOCYTE RECEPTOR; VIRUS PROTEIN;

EID: 0030943906     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00581.x     Document Type: Article
Times cited : (70)

References (42)
  • 1
    • 0028009873 scopus 로고
    • Characterization of trifluorethanol-induced partially folded state of α-lactalbumin
    • Alexandrescu, A. T., Ng, Y.-L. & Dobson, C. M. (1994) Characterization of trifluorethanol-induced partially folded state of α-lactalbumin, J. Mol. Biol. 235, 587-599.
    • (1994) J. Mol. Biol. , vol.235 , pp. 587-599
    • Alexandrescu, A.T.1    Ng, Y.-L.2    Dobson, C.M.3
  • 2
    • 0029097099 scopus 로고
    • Global fold determination from a small number of distance constraints
    • Aszodi, A., Gradwell, M. J. & Taylor, W. R. (1995) Global fold determination from a small number of distance constraints, J. Mol. Biol. 251, 308-326.
    • (1995) J. Mol. Biol. , vol.251 , pp. 308-326
    • Aszodi, A.1    Gradwell, M.J.2    Taylor, W.R.3
  • 3
    • 0021667711 scopus 로고
    • DNA sequencing with direct blotting electrophoresis
    • Beck, S. & Pohl, F. M. (1984) DNA sequencing with direct blotting electrophoresis, EMBO J. 3, 2905-2909.
    • (1984) EMBO J. , vol.3 , pp. 2905-2909
    • Beck, S.1    Pohl, F.M.2
  • 5
    • 48549112001 scopus 로고
    • Selection of coherence-transfer pathways in NMR pulse experiments
    • Bodenhausen, G., Kogler, H. & Ernst, R. R. (1984) Selection of coherence-transfer pathways in NMR pulse experiments, J. Magn. Reson. 58, 370-388.
    • (1984) J. Magn. Reson. , vol.58 , pp. 370-388
    • Bodenhausen, G.1    Kogler, H.2    Ernst, R.R.3
  • 6
    • 0028913817 scopus 로고
    • The human immunodeficiency virus type 1 (HIV-1) CD4 receptor and its central role in promotion of HIV-1 infection
    • Bour, S., Geleziunas, R. & Wainberg, M. A. (1995a) The human immunodeficiency virus type 1 (HIV-1) CD4 receptor and its central role in promotion of HIV-1 infection, Microbiol. Rev. 59, 63-93.
    • (1995) Microbiol. Rev. , vol.59 , pp. 63-93
    • Bour, S.1    Geleziunas, R.2    Wainberg, M.A.3
  • 7
    • 0028816432 scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: Implications for the mechanism of degradation
    • Bour, S., Schubert, U. & Strebel, K. (1995b) The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: Implications for the mechanism of degradation, J. Virol. 69, 1510-1520.
    • (1995) J. Virol. , vol.69 , pp. 1510-1520
    • Bour, S.1    Schubert, U.2    Strebel, K.3
  • 8
    • 0030052467 scopus 로고    scopus 로고
    • The envelope glycoprotein of human immunodeficiency virus type 2 enhances viral particle release
    • Bour, S., Schubert, U., Peden, K. & Strebel, K. (1996) The envelope glycoprotein of human immunodeficiency virus type 2 enhances viral particle release, J. Virol. 70, 820-829.
    • (1996) J. Virol. , vol.70 , pp. 820-829
    • Bour, S.1    Schubert, U.2    Peden, K.3    Strebel, K.4
  • 9
    • 0003769049 scopus 로고
    • Yale University Press, New Haven
    • Brünger, A. (1993) X-PLOR manual, Yale University Press, New Haven.
    • (1993) X-PLOR Manual
    • Brünger, A.1
  • 10
    • 0027174989 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces degradation of CD4 in vitro: The cytoplasmic domain of CD4 contributes to Vpu sensitivity
    • Chen, M. Y., Maldarelli, F., Karczewski, M. K., Willey, R. L. & Strebel, K. (1993) Human immunodeficiency virus type 1 Vpu protein induces degradation of CD4 in vitro: the cytoplasmic domain of CD4 contributes to Vpu sensitivity, J. Virol. 67, 3877-3884.
    • (1993) J. Virol. , vol.67 , pp. 3877-3884
    • Chen, M.Y.1    Maldarelli, F.2    Karczewski, M.K.3    Willey, R.L.4    Strebel, K.5
  • 11
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins
    • Chou, P. Y. & Fasman, G. (1974) Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins, Biochemistry 13, 211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.2
  • 13
    • 0029794387 scopus 로고    scopus 로고
    • The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels
    • Ewart, G. D., Sutherland, T., Cage, P. W. & Cox, G. B. (1996) The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels, J. Virol. 70, 7108-7115.
    • (1996) J. Virol. , vol.70 , pp. 7108-7115
    • Ewart, G.D.1    Sutherland, T.2    Cage, P.W.3    Cox, G.B.4
  • 14
    • 0023555768 scopus 로고
    • Further developments of protein secondary structure prediction using information theory
    • Gibrat, J. F., Garnier, J. & Robson, B. (1987) Further developments of protein secondary structure prediction using information theory, J. Mol. Biol. 198, 425-443.
    • (1987) J. Mol. Biol. , vol.198 , pp. 425-443
    • Gibrat, J.F.1    Garnier, J.2    Robson, B.3
  • 17
    • 0026605537 scopus 로고
    • CLUSTAL V: Improved software for multiple sequence alignments
    • Higgins, D. G., Bleasby, A. J. & Fuchs, R. (1992) CLUSTAL V: improved software for multiple sequence alignments, Comput. Appl. Biosci. 8, 189-191.
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 18
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features, Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 19
    • 0025917206 scopus 로고
    • Investigation of the solution structure of the human parathyroid hormone fragment (1-34) by 1H NMR spectroscopy, distance geometry, and molecular dynamics calculations
    • Klaus, W., Dieckmann, T. Wray, V., Schomburg, D., Wingender, E. & Mayor, H. (1991) Investigation of the solution structure of the human parathyroid hormone fragment (1-34) by 1H NMR spectroscopy, distance geometry, and molecular dynamics calculations, Biochemistry 30, 6936-6942.
    • (1991) Biochemistry , vol.30 , pp. 6936-6942
    • Klaus, W.1    Dieckmann, T.2    Wray, V.3    Schomburg, D.4    Wingender, E.5    Mayor, H.6
  • 20
    • 0030587419 scopus 로고    scopus 로고
    • Interaction of the cytoplasmic domains of HIV-1 Vpu and CD4: Role of Vpu residues involved in CD4 interaction and in vitro degradation
    • Margottin, F., Benichou, S., Durand, H., Richard, V., Liu, L. X., Gomas, E. & Benarous, R. (1996) Interaction of the cytoplasmic domains of HIV-1 Vpu and CD4: role of Vpu residues involved in CD4 interaction and in vitro degradation, Virology 223, 381-386.
    • (1996) Virology , vol.223 , pp. 381-386
    • Margottin, F.1    Benichou, S.2    Durand, H.3    Richard, V.4    Liu, L.X.5    Gomas, E.6    Benarous, R.7
  • 25
    • 0029186289 scopus 로고
    • TOPITS: Threading one-dimensional prediction into three-dimensional structures
    • (Rawlings, C., Clark, D., Altman, R., Hunter, L., Lengauer, T. & Wodak, S., eds) AAAI Press, Menlo Park CA
    • Rost, B. (1995) TOPITS: threading one-dimensional prediction into three-dimensional structures, The third international conference on intelligent systems for molecular biology (ISMB) (Rawlings, C., Clark, D., Altman, R., Hunter, L., Lengauer, T. & Wodak, S., eds) pp. 314-321, AAAI Press, Menlo Park CA.
    • (1995) The Third International Conference on Intelligent Systems for Molecular Biology (ISMB) , pp. 314-321
    • Rost, B.1
  • 26
    • 0027291015 scopus 로고
    • Prediction of protein structure at better than 70% accuracy
    • Rost, B. & Sander, C. (1993) Prediction of protein structure at better than 70% accuracy, J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 27
    • 0028902788 scopus 로고
    • Prediction of helical transmembrane segments at 95% accuracy
    • Rost, B., Casadio, R., Fariselli, P. & Sander, C. (1995) Prediction of helical transmembrane segments at 95% accuracy, Protein Sci. 4, 521-533.
    • (1995) Protein Sci. , vol.4 , pp. 521-533
    • Rost, B.1    Casadio, R.2    Fariselli, P.3    Sander, C.4
  • 31
    • 0028349047 scopus 로고
    • Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartiments
    • Schubert, U. & Strebel, K. (1994) Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartiments, J. Virol. 68, 2260-2271.
    • (1994) J. Virol. , vol.68 , pp. 2260-2271
    • Schubert, U.1    Strebel, K.2
  • 32
    • 0028348370 scopus 로고
    • The human immunodeficiency virus type 1 encoded Vpu protein is phosphorylated by casein kinase-2 (CK-2) at positions Ser52 and Ser56 within a predicted α-helix-turn α-helix-motif
    • Schubert, U., Henklein, P., Boldyreff, B., Wingender, E., Strebel, K. & Forstmann, T. (1994) The human immunodeficiency virus type 1 encoded Vpu protein is phosphorylated by casein kinase-2 (CK-2) at positions Ser52 and Ser56 within a predicted α-helix-turn α-helix-motif, J. Mol. Biol. 216, 16-25.
    • (1994) J. Mol. Biol. , vol.216 , pp. 16-25
    • Schubert, U.1    Henklein, P.2    Boldyreff, B.3    Wingender, E.4    Strebel, K.5    Forstmann, T.6
  • 33
    • 0030069139 scopus 로고    scopus 로고
    • The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two seperable domains
    • Schubert, U., Bour, S., Ferrer-Montiel, A. V., Montal, M., Maldarelli, M. & Strebel, K. (1996) The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two seperable domains, J. Virol. 70, 809-819.
    • (1996) J. Virol. , vol.70 , pp. 809-819
    • Schubert, U.1    Bour, S.2    Ferrer-Montiel, A.V.3    Montal, M.4    Maldarelli, M.5    Strebel, K.6
  • 34
    • 0027787871 scopus 로고
    • The crystal structure of Lysin, a fertilization protein
    • Shaw, A., McRee, E., Vacquier, V. D. & Stout, C. D. (1993) The crystal structure of Lysin, a fertilization protein, Science 262, 1864-1867.
    • (1993) Science , vol.262 , pp. 1864-1867
    • Shaw, A.1    McRee, E.2    Vacquier, V.D.3    Stout, C.D.4
  • 35
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein structure: An NMR and CD study using a synthetic actin peptide
    • Sönnichsen, F. D., van Eyck, J. E., Hodges, R. S. & Sykes, B. D. (1992) Effect of trifluoroethanol on protein structure: an NMR and CD study using a synthetic actin peptide, Biochemistry 31, 8790-8798.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sönnichsen, F.D.1    Van Eyck, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 36
    • 0028097046 scopus 로고
    • Trifluoroethanol stabilizes a helix-turn-helix motif in equine-infectious-anemia-virus trans-activator protein
    • Sticht, H., Willbold, D., Ejchart, A., Rosin-Arbesfeld, R. & Rösch, P. (1994) Trifluoroethanol stabilizes a helix-turn-helix motif in equine-infectious-anemia-virus trans-activator protein, Eur. J. Biochem. 225, 855-861.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 855-861
    • Sticht, H.1    Willbold, D.2    Ejchart, A.3    Rosin-Arbesfeld, R.4    Rösch, P.5
  • 38
    • 0028820287 scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein: A potential regulator of proteolysis and protein transport in the mammalian secretory pathway
    • Vincent, M. J. & Jabbar, M. A. (1995) The human immunodeficiency virus type 1 Vpu protein: A potential regulator of proteolysis and protein transport in the mammalian secretory pathway, Virology 214, 639-649.
    • (1995) Virology , vol.214 , pp. 639-649
    • Vincent, M.J.1    Jabbar, M.A.2
  • 39
    • 0028306105 scopus 로고
    • Structure of the equine infectious anemia virus Tat protein
    • Willbold, D., Rosin-Arbesfeld, R., Sticht, H., Frank, R. & Pösch, P. (1994) Structure of the equine infectious anemia virus Tat protein, Science 264, 1584-1587.
    • (1994) Science , vol.264 , pp. 1584-1587
    • Willbold, D.1    Rosin-Arbesfeld, R.2    Sticht, H.3    Frank, R.4    Pösch, P.5
  • 40
    • 0030511919 scopus 로고    scopus 로고
    • Solution structure of the human CD4 (403-419) receptor peptide
    • Willbold, D. & Rösch, P. (1996) Solution structure of the human CD4 (403-419) receptor peptide, J. Biomed. Sci. 3, 435-441.
    • (1996) J. Biomed. Sci. , vol.3 , pp. 435-441
    • Willbold, D.1    Rösch, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.