메뉴 건너뛰기




Volumn 273, Issue 5272, 1996, Pages 231-235

Structure of the amino-terminal core domain of the HIV-1 capsid protein

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN;

EID: 0029794123     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5272.231     Document Type: Article
Times cited : (411)

References (107)
  • 1
    • 0025728301 scopus 로고
    • J. Wills and R. Craven, AIDS 5, 639 (1991); H. Gelderblom et al., Membrane Interactions of HIV, R. C. Aloa and C. C. Curtain, Eds. (Wiley-Liss, New York, 1992), pp 33-54; S. Modrow et al., Med. Microbiol. Immunol. Berlin 184, 177 (1994); E. Hunter, Semin. Virol. 5, 71 (1994).
    • (1991) AIDS , vol.5 , pp. 639
    • Wills, J.1    Craven, R.2
  • 2
    • 0025728301 scopus 로고
    • R. C. Aloa and C. C. Curtain, Eds. Wiley-Liss, New York
    • J. Wills and R. Craven, AIDS 5, 639 (1991); H. Gelderblom et al., Membrane Interactions of HIV, R. C. Aloa and C. C. Curtain, Eds. (Wiley-Liss, New York, 1992), pp 33-54; S. Modrow et al., Med. Microbiol. Immunol. Berlin 184, 177 (1994); E. Hunter, Semin. Virol. 5, 71 (1994).
    • (1992) Membrane Interactions of HIV , pp. 33-54
    • Gelderblom, H.1
  • 3
    • 0025728301 scopus 로고
    • J. Wills and R. Craven, AIDS 5, 639 (1991); H. Gelderblom et al., Membrane Interactions of HIV, R. C. Aloa and C. C. Curtain, Eds. (Wiley-Liss, New York, 1992), pp 33-54; S. Modrow et al., Med. Microbiol. Immunol. Berlin 184, 177 (1994); E. Hunter, Semin. Virol. 5, 71 (1994).
    • (1994) Med. Microbiol. Immunol. Berlin , vol.184 , pp. 177
    • Modrow, S.1
  • 4
    • 0002168907 scopus 로고
    • J. Wills and R. Craven, AIDS 5, 639 (1991); H. Gelderblom et al., Membrane Interactions of HIV, R. C. Aloa and C. C. Curtain, Eds. (Wiley-Liss, New York, 1992), pp 33-54; S. Modrow et al., Med. Microbiol. Immunol. Berlin 184, 177 (1994); E. Hunter, Semin. Virol. 5, 71 (1994).
    • (1994) Semin. Virol. , vol.5 , pp. 71
    • Hunter, E.1
  • 5
    • 0023755462 scopus 로고
    • R. J. Mervis et al., J. Virol. 62, 3993 (1988), L. E. Henderson et al., ibid. 66, 1856 (1992).
    • (1988) J. Virol. , vol.62 , pp. 3993
    • Mervis, R.J.1
  • 6
    • 0026515142 scopus 로고
    • R. J. Mervis et al., J. Virol. 62, 3993 (1988), L. E. Henderson et al., ibid. 66, 1856 (1992).
    • (1992) J. Virol. , vol.66 , pp. 1856
    • Henderson, L.E.1
  • 7
    • 0342394457 scopus 로고    scopus 로고
    • H. G. Göttlinger, J. G. Sodroski, W. A. Haseltine, Proc. Natl. Acad. Sci. U.S.A. 86, 5781 (1989); J. Jowett, D. Hockley, M. V. Nermut, I. M. Jones, J. Gen. Virol. 73, 3079 (1992); A. von Poblotzki et al., Virology 193, 981 (1993); S. S. Hong and P. Boulanger, J. Virol. 67, 2787 (1993), C.-T. Wang and E. Barklis, ibid., p. 4264; E. K. Franke, H. En Hui Yuan, K. L. Bossolt, S. P. Goff, J. Luban, ibid. 68, 5300 (1994); N. Chazal, C. Carriere, B. Gay, P. Boulanger, ibid. , p. 111; P. Spearman, J. J. Wang, H. N. Vander, L. Ratner, ibid. , p. 3232.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 5781
    • Göttlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 8
    • 0027101766 scopus 로고
    • H. G. Göttlinger, J. G. Sodroski, W. A. Haseltine, Proc. Natl. Acad. Sci. U.S.A. 86, 5781 (1989); J. Jowett, D. Hockley, M. V. Nermut, I. M. Jones, J. Gen. Virol. 73, 3079 (1992); A. von Poblotzki et al., Virology 193, 981 (1993); S. S. Hong and P. Boulanger, J. Virol. 67, 2787 (1993), C.-T. Wang and E. Barklis, ibid., p. 4264; E. K. Franke, H. En Hui Yuan, K. L. Bossolt, S. P. Goff, J. Luban, ibid. 68, 5300 (1994); N. Chazal, C. Carriere, B. Gay, P. Boulanger, ibid. , p. 111; P. Spearman, J. J. Wang, H. N. Vander, L. Ratner, ibid. , p. 3232.
    • (1992) J. Gen. Virol. , vol.73 , pp. 3079
    • Jowett, J.1    Hockley, D.2    Nermut, M.V.3    Jones, I.M.4
  • 9
    • 0027335896 scopus 로고
    • H. G. Göttlinger, J. G. Sodroski, W. A. Haseltine, Proc. Natl. Acad. Sci. U.S.A. 86, 5781 (1989); J. Jowett, D. Hockley, M. V. Nermut, I. M. Jones, J. Gen. Virol. 73, 3079 (1992); A. von Poblotzki et al., Virology 193, 981 (1993); S. S. Hong and P. Boulanger, J. Virol. 67, 2787 (1993), C.-T. Wang and E. Barklis, ibid., p. 4264; E. K. Franke, H. En Hui Yuan, K. L. Bossolt, S. P. Goff, J. Luban, ibid. 68, 5300 (1994); N. Chazal, C. Carriere, B. Gay, P. Boulanger, ibid. , p. 111; P. Spearman, J. J. Wang, H. N. Vander, L. Ratner, ibid. , p. 3232.
    • (1993) Virology , vol.193 , pp. 981
    • Von Poblotzki, A.1
  • 10
    • 0027412453 scopus 로고
    • H. G. Göttlinger, J. G. Sodroski, W. A. Haseltine, Proc. Natl. Acad. Sci. U.S.A. 86, 5781 (1989); J. Jowett, D. Hockley, M. V. Nermut, I. M. Jones, J. Gen. Virol. 73, 3079 (1992); A. von Poblotzki et al., Virology 193, 981 (1993); S. S. Hong and P. Boulanger, J. Virol. 67, 2787 (1993), C.-T. Wang and E. Barklis, ibid., p. 4264; E. K. Franke, H. En Hui Yuan, K. L. Bossolt, S. P. Goff, J. Luban, ibid. 68, 5300 (1994); N. Chazal, C. Carriere, B. Gay, P. Boulanger, ibid. , p. 111; P. Spearman, J. J. Wang, H. N. Vander, L. Ratner, ibid. , p. 3232.
    • (1993) J. Virol. , vol.67 , pp. 2787
    • Hong, S.S.1    Boulanger, P.2
  • 11
    • 0342394457 scopus 로고    scopus 로고
    • H. G. Göttlinger, J. G. Sodroski, W. A. Haseltine, Proc. Natl. Acad. Sci. U.S.A. 86, 5781 (1989); J. Jowett, D. Hockley, M. V. Nermut, I. M. Jones, J. Gen. Virol. 73, 3079 (1992); A. von Poblotzki et al., Virology 193, 981 (1993); S. S. Hong and P. Boulanger, J. Virol. 67, 2787 (1993), C.-T. Wang and E. Barklis, ibid., p. 4264; E. K. Franke, H. En Hui Yuan, K. L. Bossolt, S. P. Goff, J. Luban, ibid. 68, 5300 (1994); N. Chazal, C. Carriere, B. Gay, P. Boulanger, ibid. , p. 111; P. Spearman, J. J. Wang, H. N. Vander, L. Ratner, ibid. , p. 3232.
    • J. Virol. , pp. 4264
    • Wang, C.-T.1    Barklis, E.2
  • 12
    • 0028363103 scopus 로고
    • H. G. Göttlinger, J. G. Sodroski, W. A. Haseltine, Proc. Natl. Acad. Sci. U.S.A. 86, 5781 (1989); J. Jowett, D. Hockley, M. V. Nermut, I. M. Jones, J. Gen. Virol. 73, 3079 (1992); A. von Poblotzki et al., Virology 193, 981 (1993); S. S. Hong and P. Boulanger, J. Virol. 67, 2787 (1993), C.-T. Wang and E. Barklis, ibid., p. 4264; E. K. Franke, H. En Hui Yuan, K. L. Bossolt, S. P. Goff, J. Luban, ibid. 68, 5300 (1994); N. Chazal, C. Carriere, B. Gay, P. Boulanger, ibid. , p. 111; P. Spearman, J. J. Wang, H. N. Vander, L. Ratner, ibid. , p. 3232.
    • (1994) J. Virol. , vol.68 , pp. 5300
    • Franke, E.K.1    En Hui Yuan, H.2    Bossolt, K.L.3    Goff, S.P.4    Luban, J.5
  • 13
    • 0342394457 scopus 로고    scopus 로고
    • H. G. Göttlinger, J. G. Sodroski, W. A. Haseltine, Proc. Natl. Acad. Sci. U.S.A. 86, 5781 (1989); J. Jowett, D. Hockley, M. V. Nermut, I. M. Jones, J. Gen. Virol. 73, 3079 (1992); A. von Poblotzki et al., Virology 193, 981 (1993); S. S. Hong and P. Boulanger, J. Virol. 67, 2787 (1993), C.-T. Wang and E. Barklis, ibid., p. 4264; E. K. Franke, H. En Hui Yuan, K. L. Bossolt, S. P. Goff, J. Luban, ibid. 68, 5300 (1994); N. Chazal, C. Carriere, B. Gay, P. Boulanger, ibid. , p. 111; P. Spearman, J. J. Wang, H. N. Vander, L. Ratner, ibid. , p. 3232.
    • J. Virol. , pp. 111
    • Chazal, N.1    Carriere, C.2    Gay, B.3    Boulanger, P.4
  • 14
    • 0342394457 scopus 로고    scopus 로고
    • H. G. Göttlinger, J. G. Sodroski, W. A. Haseltine, Proc. Natl. Acad. Sci. U.S.A. 86, 5781 (1989); J. Jowett, D. Hockley, M. V. Nermut, I. M. Jones, J. Gen. Virol. 73, 3079 (1992); A. von Poblotzki et al., Virology 193, 981 (1993); S. S. Hong and P. Boulanger, J. Virol. 67, 2787 (1993), C.-T. Wang and E. Barklis, ibid., p. 4264; E. K. Franke, H. En Hui Yuan, K. L. Bossolt, S. P. Goff, J. Luban, ibid. 68, 5300 (1994); N. Chazal, C. Carriere, B. Gay, P. Boulanger, ibid. , p. 111; P. Spearman, J. J. Wang, H. N. Vander, L. Ratner, ibid. , p. 3232.
    • J. Virol. , pp. 3232
    • Spearman, P.1    Wang, J.J.2    Vander, H.N.3    Ratner, L.4
  • 19
    • 0029949799 scopus 로고    scopus 로고
    • E. K. Franke, H. En Hui Yuan, J. Luban, Nature 372, 359 (1994); D. Braaten, E. K. Franke, J. Luban, J. Virol. 70, 3551 (1996).
    • (1996) J. Virol. , vol.70 , pp. 3551
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 20
    • 0027971782 scopus 로고
    • M. Thali et al., Nature 372, 363 (1994).
    • (1994) Nature , vol.372 , pp. 363
    • Thali, M.1
  • 21
    • 0028965266 scopus 로고
    • A. Billich et al., J. Virol. 69, 2451 (1995); D. E. Ott et al., AIDS Res. Hum. Petroviruses 11, 1003 (1995).
    • (1995) J. Virol. , vol.69 , pp. 2451
    • Billich, A.1
  • 22
  • 23
    • 0021159379 scopus 로고    scopus 로고
    • R. E. Handschumacher, M. W. Harding, J. Rice, R. J. Drugge, Science 226, 544 (1984); G. Fischer, B. Wittmann-Liebold, K. Lang, T. Kiefhaber, F. X. Schmid, Nature 337, 476 (1989); Y. Thériault et al., ibid. 361, 88 (1993); G. Pflügl et al., ibid., p. 91.
    • (1984) Science , vol.226 , pp. 544
    • Handschumacher, R.E.1    Harding, M.W.2    Rice, J.3    Drugge, R.J.4
  • 24
    • 0024959449 scopus 로고
    • R. E. Handschumacher, M. W. Harding, J. Rice, R. J. Drugge, Science 226, 544 (1984); G. Fischer, B. Wittmann-Liebold, K. Lang, T. Kiefhaber, F. X. Schmid, Nature 337, 476 (1989); Y. Thériault et al., ibid. 361, 88 (1993); G. Pflügl et al., ibid., p. 91.
    • (1989) Nature , vol.337 , pp. 476
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 25
    • 0021159379 scopus 로고    scopus 로고
    • R. E. Handschumacher, M. W. Harding, J. Rice, R. J. Drugge, Science 226, 544 (1984); G. Fischer, B. Wittmann-Liebold, K. Lang, T. Kiefhaber, F. X. Schmid, Nature 337, 476 (1989); Y. Thériault et al., ibid. 361, 88 (1993); G. Pflügl et al., ibid., p. 91.
    • (1993) Ibid. , vol.361 , pp. 88
    • Thériault, Y.1
  • 26
    • 0021159379 scopus 로고    scopus 로고
    • R. E. Handschumacher, M. W. Harding, J. Rice, R. J. Drugge, Science 226, 544 (1984); G. Fischer, B. Wittmann-Liebold, K. Lang, T. Kiefhaber, F. X. Schmid, Nature 337, 476 (1989); Y. Thériault et al., ibid. 361, 88 (1993); G. Pflügl et al., ibid., p. 91.
    • Ibid. , pp. 91
    • Pflügl, G.1
  • 28
    • 0026762403 scopus 로고
    • L. S. Ehrlich, B. E. Agresta, C. A. Carter, ibid. 66, 4874 (1992); S. Rosé et al., Proteins Struct. Funct. Genet. 13, 112 (1992); I. Brooks, D. G. Watts, K. K. Soneson, P. Hensley, Methods Enzymol. 240, 459 (1994).
    • (1992) J. Virol. , vol.66 , pp. 4874
    • Ehrlich, L.S.1    Agresta, B.E.2    Carter, C.A.3
  • 29
    • 0026682511 scopus 로고
    • L. S. Ehrlich, B. E. Agresta, C. A. Carter, ibid. 66, 4874 (1992); S. Rosé et al., Proteins Struct. Funct. Genet. 13, 112 (1992); I. Brooks, D. G. Watts, K. K. Soneson, P. Hensley, Methods Enzymol. 240, 459 (1994).
    • (1992) Proteins Struct. Funct. Genet. , vol.13 , pp. 112
    • Rosé, S.1
  • 30
    • 0028672974 scopus 로고
    • L. S. Ehrlich, B. E. Agresta, C. A. Carter, ibid. 66, 4874 (1992); S. Rosé et al., Proteins Struct. Funct. Genet. 13, 112 (1992); I. Brooks, D. G. Watts, K. K. Soneson, P. Hensley, Methods Enzymol. 240, 459 (1994).
    • (1994) Methods Enzymol. , vol.240 , pp. 459
    • Brooks, I.1    Watts, D.G.2    Soneson, K.K.3    Hensley, P.4
  • 33
    • 9444283436 scopus 로고    scopus 로고
    • note
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
  • 37
    • 34249765651 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1994) J. Biomol. NMR , vol.4 , pp. 603
    • Johnson, B.A.1    Blevins, R.A.2
  • 38
    • 0027787894 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593
    • Grzesiek, S.1    Bax, A.2
  • 39
    • 0026951903 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1992) J. Biomol. NMR , vol.2 , pp. 661
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 40
    • 44049117010 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1992) J. Magn. Reson. , vol.96 , pp. 432
    • Grzesiek, S.1    Bax, A.2
  • 41
    • 9444245493 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291
  • 42
    • 43949175202 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1993) J. Magn. Reson. B , vol.101 , pp. 114
    • Grzesiek, S.1    Anglister, J.2    Bax, A.3
  • 43
    • 0001689741 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1994) J. Magn. Reson. B , vol.103 , pp. 203
    • Muhandiram, D.R.1    Kay, L.2
  • 44
    • 44949291986 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1990) J. Magn. Reson. , vol.89 , pp. 496
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 45
    • 0026225733 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1991) J. Biomol. NMR , vol.1 , pp. 299
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 46
    • 44949288628 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1990) J. Magn. Reson. , vol.88 , pp. 425
    • Bax, A.1    Clore, G.M.2    Gronenbom, A.M.3
  • 50
    • 84915716471 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1980) Mol. Phys. , vol.41 , pp. 95
    • Macura, S.1    Ernst, R.R.2
  • 53
    • 0013498057 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1993) J. Magn. Reson. B , vol.101 , pp. 210
    • Vuister, G.1
  • 54
    • 0024988099 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1990) Science , vol.249 , pp. 411
    • Kay, L.E.1    Clore, G.M.2    Bax, A.3    Gronenborn, A.M.4
  • 55
    • 0000045562 scopus 로고
    • 15N edited HMQC-NOESY-HSQC data [L. E. Kay, G. M. Clore, A. Bax, A. M. Gronenborn, Science 249, 411 (1990); D. R. Muhandiram, G. Y. Xu, L. E. Kay, J. Biomol. NMR 3, 463 (1993)].
    • (1993) J. Biomol. NMR , vol.3 , pp. 463
    • Muhandiram, D.R.1    Xu, G.Y.2    Kay, L.E.3
  • 56
    • 0026089657 scopus 로고
    • 2 and best-fit backbone root mean square (rms) deviations of 1.3 ± 0.3 Å. Backbone hydrogen bond restraints identified with the use of DIANA, and additional NOE restraints, were included in subsequent rounds of refinement, which led to improved convergence but did not alter the global fold. Color figures were generated with the Midas-plus [T. E. Ferrin, C. C. Huang, L. E. Jarvis, R. Langridge, J. Mol. Graph. 6, 13 (1988], Molscript [P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991)], and Raster-3D [D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994)] software packages.
    • (1991) J. Mol. Biol. , vol.217 , pp. 517
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 57
    • 0026259488 scopus 로고
    • 2 and best-fit backbone root mean square (rms) deviations of 1.3 ± 0.3 Å. Backbone hydrogen bond restraints identified with the use of DIANA, and additional NOE restraints, were included in subsequent rounds of refinement, which led to improved convergence but did not alter the global fold. Color figures were generated with the Midas-plus [T. E. Ferrin, C. C. Huang, L. E. Jarvis, R. Langridge, J. Mol. Graph. 6, 13 (1988], Molscript [P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991)], and Raster-3D [D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994)] software packages.
    • (1991) J. Biomol. NMR , vol.1 , pp. 447
    • Güntert, P.1    Wüthrich, K.2
  • 58
    • 0026089657 scopus 로고
    • Wiley, New York
    • 2 and best-fit backbone root mean square (rms) deviations of 1.3 ± 0.3 Å. Backbone hydrogen bond restraints identified with the use of DIANA, and additional NOE restraints, were included in subsequent rounds of refinement, which led to improved convergence but did not alter the global fold. Color figures were generated with the Midas-plus [T. E. Ferrin, C. C. Huang, L. E. Jarvis, R. Langridge, J. Mol. Graph. 6, 13 (1988], Molscript [P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991)], and Raster-3D [D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994)] software packages.
    • (1986) NMR of Proteins and Nucleic Acids
    • Wüthrich, K.1
  • 59
    • 0347610773 scopus 로고
    • 2 and best-fit backbone root mean square (rms) deviations of 1.3 ± 0.3 Å. Backbone hydrogen bond restraints identified with the use of DIANA, and additional NOE restraints, were included in subsequent rounds of refinement, which led to improved convergence but did not alter the global fold. Color figures were generated with the Midas-plus [T. E. Ferrin, C. C. Huang, L. E. Jarvis, R. Langridge, J. Mol. Graph. 6, 13 (1988], Molscript [P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991)], and Raster-3D [D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994)] software packages.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490
    • Spera, S.1    Bax, A.2
  • 60
    • 0026410969 scopus 로고
    • 2 and best-fit backbone root mean square (rms) deviations of 1.3 ± 0.3 Å. Backbone hydrogen bond restraints identified with the use of DIANA, and additional NOE restraints, were included in subsequent rounds of refinement, which led to improved convergence but did not alter the global fold. Color figures were generated with the Midas-plus [T. E. Ferrin, C. C. Huang, L. E. Jarvis, R. Langridge, J. Mol. Graph. 6, 13 (1988], Molscript [P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991)], and Raster-3D [D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994)] software packages.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 61
    • 0026597879 scopus 로고
    • 2 and best-fit backbone root mean square (rms) deviations of 1.3 ± 0.3 Å. Backbone hydrogen bond restraints identified with the use of DIANA, and additional NOE restraints, were included in subsequent rounds of refinement, which led to improved convergence but did not alter the global fold. Color figures were generated with the Midas-plus [T. E. Ferrin, C. C. Huang, L. E. Jarvis, R. Langridge, J. Mol. Graph. 6, 13 (1988], Molscript [P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991)], and Raster-3D [D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994)] software packages.
    • (1992) Biochemistry , vol.31 , pp. 1647
  • 62
    • 0028393784 scopus 로고
    • 2 and best-fit backbone root mean square (rms) deviations of 1.3 ± 0.3 Å. Backbone hydrogen bond restraints identified with the use of DIANA, and additional NOE restraints, were included in subsequent rounds of refinement, which led to improved convergence but did not alter the global fold. Color figures were generated with the Midas-plus [T. E. Ferrin, C. C. Huang, L. E. Jarvis, R. Langridge, J. Mol. Graph. 6, 13 (1988], Molscript [P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991)], and Raster-3D [D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994)] software packages.
    • (1994) J. Biomol. NMR , vol.4 , pp. 171
    • Wishart, D.S.1    Sykes, B.D.2
  • 63
    • 0023977089 scopus 로고
    • 2 and best-fit backbone root mean square (rms) deviations of 1.3 ± 0.3 Å. Backbone hydrogen bond restraints identified with the use of DIANA, and additional NOE restraints, were included in subsequent rounds of refinement, which led to improved convergence but did not alter the global fold. Color figures were generated with the Midas-plus [T. E. Ferrin, C. C. Huang, L. E. Jarvis, R. Langridge, J. Mol. Graph. 6, 13 (1988], Molscript [P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991)], and Raster-3D [D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994)] software packages.
    • (1988) J. Mol. Graph. , vol.6 , pp. 13
    • Ferrin, T.E.1    Huang, C.C.2    Jarvis, L.E.3    Langridge, R.4
  • 64
    • 0026089657 scopus 로고
    • 2 and best-fit backbone root mean square (rms) deviations of 1.3 ± 0.3 Å. Backbone hydrogen bond restraints identified with the use of DIANA, and additional NOE restraints, were included in subsequent rounds of refinement, which led to improved convergence but did not alter the global fold. Color figures were generated with the Midas-plus [T. E. Ferrin, C. C. Huang, L. E. Jarvis, R. Langridge, J. Mol. Graph. 6, 13 (1988], Molscript [P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991)], and Raster-3D [D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994)] software packages.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946
    • Kraulis, P.J.1
  • 65
    • 0026089657 scopus 로고
    • 2 and best-fit backbone root mean square (rms) deviations of 1.3 ± 0.3 Å. Backbone hydrogen bond restraints identified with the use of DIANA, and additional NOE restraints, were included in subsequent rounds of refinement, which led to improved convergence but did not alter the global fold. Color figures were generated with the Midas-plus [T. E. Ferrin, C. C. Huang, L. E. Jarvis, R. Langridge, J. Mol. Graph. 6, 13 (1988], Molscript [P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991)], and Raster-3D [D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994)] software packages.
    • (1988) J. Mol. Graph. , vol.6 , pp. 219
    • Bacon, D.J.1    Anderson, W.F.2
  • 66
    • 0028057108 scopus 로고
    • 2 and best-fit backbone root mean square (rms) deviations of 1.3 ± 0.3 Å. Backbone hydrogen bond restraints identified with the use of DIANA, and additional NOE restraints, were included in subsequent rounds of refinement, which led to improved convergence but did not alter the global fold. Color figures were generated with the Midas-plus [T. E. Ferrin, C. C. Huang, L. E. Jarvis, R. Langridge, J. Mol. Graph. 6, 13 (1988], Molscript [P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991)], and Raster-3D [D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994)] software packages.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 67
    • 0000950943 scopus 로고
    • Backbone NH protons that undergo rapid exchange with water protons were identified from MEXICO NMR data [G. Gemmecker, W. Jahnke, H. Kessler, J. Am. Chem. Soc. 115, 11620 (1993); S. Koide, W. Jahnke, P. E. Wright, J. Biomol. NMR 6, 306 (1995)] collected with exchange intervals of 25, 50, 75, and 100 ms.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11620
    • Gemmecker, G.1    Jahnke, W.2    Kessler, H.3
  • 68
    • 0029396845 scopus 로고
    • Backbone NH protons that undergo rapid exchange with water protons were identified from MEXICO NMR data [G. Gemmecker, W. Jahnke, H. Kessler, J. Am. Chem. Soc. 115, 11620 (1993); S. Koide, W. Jahnke, P. E. Wright, J. Biomol. NMR 6, 306 (1995)] collected with exchange intervals of 25, 50, 75, and 100 ms.
    • (1995) J. Biomol. NMR , vol.6 , pp. 306
    • Koide, S.1    Jahnke, W.2    Wright, P.E.3
  • 69
    • 0027440362 scopus 로고
    • A search of the Brookhaven Protein Data Bank for homologous structures with the DALI program [L. Holm and C. Sander, J. Mol. Biol. 233, 123 (1993)] revealed homotetrameric cyanomet hemoglobin from the innkeeper worm Urechis caupo [P. R. Kolatkar et al., Acta Crystallogr. B48, 191 (1992)] as the only potential homolog (best-fit rms deviations = 6.5 Å, z = 2.0).
    • (1993) J. Mol. Biol. , vol.233 , pp. 123
    • Holm, L.1    Sander, C.2
  • 70
    • 4244115091 scopus 로고
    • A search of the Brookhaven Protein Data Bank for homologous structures with the DALI program [L. Holm and C. Sander, J. Mol. Biol. 233, 123 (1993)] revealed homotetrameric cyanomet hemoglobin from the innkeeper worm Urechis caupo [P. R. Kolatkar et al., Acta Crystallogr. B48, 191 (1992)] as the only potential homolog (best-fit rms deviations = 6.5 Å, z = 2.0).
    • (1992) Acta Crystallogr. , vol.B48 , pp. 191
    • Kolatkar, P.R.1
  • 71
    • 0024322439 scopus 로고
    • For examples, see the following: M. Rossman and J. Johnson, Annu. Rev. Biochem. 58, 533 (1989); M. G. Rossmann et al., Nature 317, 145 (1985); J. M. Hogle et al., Science 229, 1358 (1985); S. C. Harrison et al., Nature 276, 368 (1978); C. Abad-Zapatero et al., ibid. 286, 33 (1980); L. Liljas et al., J. Mol. Biol. 159, 93 (1982); K. Valegard et al., Nature 345, 36 (1990); J. Grimes et al., ibid. 373, 167 (1995); A. K. Basak et al., J. Virol. 70, 3797 (1996).
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 533
    • Rossman, M.1    Johnson, J.2
  • 72
    • 0022401514 scopus 로고
    • For examples, see the following: M. Rossman and J. Johnson, Annu. Rev. Biochem. 58, 533 (1989); M. G. Rossmann et al., Nature 317, 145 (1985); J. M. Hogle et al., Science 229, 1358 (1985); S. C. Harrison et al., Nature 276, 368 (1978); C. Abad-Zapatero et al., ibid. 286, 33 (1980); L. Liljas et al., J. Mol. Biol. 159, 93 (1982); K. Valegard et al., Nature 345, 36 (1990); J. Grimes et al., ibid. 373, 167 (1995); A. K. Basak et al., J. Virol. 70, 3797 (1996).
    • (1985) Nature , vol.317 , pp. 145
    • Rossmann, M.G.1
  • 73
    • 0022409872 scopus 로고
    • For examples, see the following: M. Rossman and J. Johnson, Annu. Rev. Biochem. 58, 533 (1989); M. G. Rossmann et al., Nature 317, 145 (1985); J. M. Hogle et al., Science 229, 1358 (1985); S. C. Harrison et al., Nature 276, 368 (1978); C. Abad-Zapatero et al., ibid. 286, 33 (1980); L. Liljas et al., J. Mol. Biol. 159, 93 (1982); K. Valegard et al., Nature 345, 36 (1990); J. Grimes et al., ibid. 373, 167 (1995); A. K. Basak et al., J. Virol. 70, 3797 (1996).
    • (1985) Science , vol.229 , pp. 1358
    • Hogle, J.M.1
  • 74
    • 0018225178 scopus 로고
    • For examples, see the following: M. Rossman and J. Johnson, Annu. Rev. Biochem. 58, 533 (1989); M. G. Rossmann et al., Nature 317, 145 (1985); J. M. Hogle et al., Science 229, 1358 (1985); S. C. Harrison et al., Nature 276, 368 (1978); C. Abad-Zapatero et al., ibid. 286, 33 (1980); L. Liljas et al., J. Mol. Biol. 159, 93 (1982); K. Valegard et al., Nature 345, 36 (1990); J. Grimes et al., ibid. 373, 167 (1995); A. K. Basak et al., J. Virol. 70, 3797 (1996).
    • (1978) Nature , vol.276 , pp. 368
    • Harrison, S.C.1
  • 75
    • 0018818719 scopus 로고
    • For examples, see the following: M. Rossman and J. Johnson, Annu. Rev. Biochem. 58, 533 (1989); M. G. Rossmann et al., Nature 317, 145 (1985); J. M. Hogle et al., Science 229, 1358 (1985); S. C. Harrison et al., Nature 276, 368 (1978); C. Abad-Zapatero et al., ibid. 286, 33 (1980); L. Liljas et al., J. Mol. Biol. 159, 93 (1982); K. Valegard et al., Nature 345, 36 (1990); J. Grimes et al., ibid. 373, 167 (1995); A. K. Basak et al., J. Virol. 70, 3797 (1996).
    • (1980) Nature , vol.286 , pp. 33
    • Abad-Zapatero, C.1
  • 76
    • 0020490917 scopus 로고
    • For examples, see the following: M. Rossman and J. Johnson, Annu. Rev. Biochem. 58, 533 (1989); M. G. Rossmann et al., Nature 317, 145 (1985); J. M. Hogle et al., Science 229, 1358 (1985); S. C. Harrison et al., Nature 276, 368 (1978); C. Abad-Zapatero et al., ibid. 286, 33 (1980); L. Liljas et al., J. Mol. Biol. 159, 93 (1982); K. Valegard et al., Nature 345, 36 (1990); J. Grimes et al., ibid. 373, 167 (1995); A. K. Basak et al., J. Virol. 70, 3797 (1996).
    • (1982) J. Mol. Biol. , vol.159 , pp. 93
    • Liljas, L.1
  • 77
    • 0025344593 scopus 로고
    • For examples, see the following: M. Rossman and J. Johnson, Annu. Rev. Biochem. 58, 533 (1989); M. G. Rossmann et al., Nature 317, 145 (1985); J. M. Hogle et al., Science 229, 1358 (1985); S. C. Harrison et al., Nature 276, 368 (1978); C. Abad-Zapatero et al., ibid. 286, 33 (1980); L. Liljas et al., J. Mol. Biol. 159, 93 (1982); K. Valegard et al., Nature 345, 36 (1990); J. Grimes et al., ibid. 373, 167 (1995); A. K. Basak et al., J. Virol. 70, 3797 (1996).
    • (1990) Nature , vol.345 , pp. 36
    • Valegard, K.1
  • 78
    • 0028874050 scopus 로고
    • For examples, see the following: M. Rossman and J. Johnson, Annu. Rev. Biochem. 58, 533 (1989); M. G. Rossmann et al., Nature 317, 145 (1985); J. M. Hogle et al., Science 229, 1358 (1985); S. C. Harrison et al., Nature 276, 368 (1978); C. Abad-Zapatero et al., ibid. 286, 33 (1980); L. Liljas et al., J. Mol. Biol. 159, 93 (1982); K. Valegard et al., Nature 345, 36 (1990); J. Grimes et al., ibid. 373, 167 (1995); A. K. Basak et al., J. Virol. 70, 3797 (1996).
    • (1995) Nature , vol.373 , pp. 167
    • Grimes, J.1
  • 79
    • 0029924725 scopus 로고    scopus 로고
    • For examples, see the following: M. Rossman and J. Johnson, Annu. Rev. Biochem. 58, 533 (1989); M. G. Rossmann et al., Nature 317, 145 (1985); J. M. Hogle et al., Science 229, 1358 (1985); S. C. Harrison et al., Nature 276, 368 (1978); C. Abad-Zapatero et al., ibid. 286, 33 (1980); L. Liljas et al., J. Mol. Biol. 159, 93 (1982); K. Valegard et al., Nature 345, 36 (1990); J. Grimes et al., ibid. 373, 167 (1995); A. K. Basak et al., J. Virol. 70, 3797 (1996).
    • (1996) J. Virol. , vol.70 , pp. 3797
    • Basak, A.K.1
  • 80
    • 0023140272 scopus 로고
    • A. R. M. Coates, J. Cookson, G. J. Barton, M. J. Zvelebil, M. J. E. Sternberg, Nature 326, 549 (1987); M. G. Rossmann, Proc. Natl. Acad. Sci. U.S.A. 85, 4625 (1988); P. Argos, EMBO J. 8, 779 (1989); J. P. M. Langedijk, J. J. Schalken, M. Tersmette, J. G. Huisman, R. H. Meloen, J. Gen. Virol. 71, 2609 (1990); V. Robert-Hebmann et al., Mol. Immunol. 29, 729 (1992).
    • (1987) Nature , vol.326 , pp. 549
    • Coates, A.R.M.1    Cookson, J.2    Barton, G.J.3    Zvelebil, M.J.4    Sternberg, M.J.E.5
  • 81
    • 0008238291 scopus 로고
    • A. R. M. Coates, J. Cookson, G. J. Barton, M. J. Zvelebil, M. J. E. Sternberg, Nature 326, 549 (1987); M. G. Rossmann, Proc. Natl. Acad. Sci. U.S.A. 85, 4625 (1988); P. Argos, EMBO J. 8, 779 (1989); J. P. M. Langedijk, J. J. Schalken, M. Tersmette, J. G. Huisman, R. H. Meloen, J. Gen. Virol. 71, 2609 (1990); V. Robert-Hebmann et al., Mol. Immunol. 29, 729 (1992).
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 4625
    • Rossmann, M.G.1
  • 82
    • 0024426029 scopus 로고
    • A. R. M. Coates, J. Cookson, G. J. Barton, M. J. Zvelebil, M. J. E. Sternberg, Nature 326, 549 (1987); M. G. Rossmann, Proc. Natl. Acad. Sci. U.S.A. 85, 4625 (1988); P. Argos, EMBO J. 8, 779 (1989); J. P. M. Langedijk, J. J. Schalken, M. Tersmette, J. G. Huisman, R. H. Meloen, J. Gen. Virol. 71, 2609 (1990); V. Robert-Hebmann et al., Mol. Immunol. 29, 729 (1992).
    • (1989) EMBO J. , vol.8 , pp. 779
    • Argos, P.1
  • 83
    • 0025155226 scopus 로고
    • A. R. M. Coates, J. Cookson, G. J. Barton, M. J. Zvelebil, M. J. E. Sternberg, Nature 326, 549 (1987); M. G. Rossmann, Proc. Natl. Acad. Sci. U.S.A. 85, 4625 (1988); P. Argos, EMBO J. 8, 779 (1989); J. P. M. Langedijk, J. J. Schalken, M. Tersmette, J. G. Huisman, R. H. Meloen, J. Gen. Virol. 71, 2609 (1990); V. Robert-Hebmann et al., Mol. Immunol. 29, 729 (1992).
    • (1990) J. Gen. Virol. , vol.71 , pp. 2609
    • Langedijk, J.P.M.1    Schalken, J.J.2    Tersmette, M.3    Huisman, J.G.4    Meloen, R.H.5
  • 84
    • 0026704684 scopus 로고
    • A. R. M. Coates, J. Cookson, G. J. Barton, M. J. Zvelebil, M. J. E. Sternberg, Nature 326, 549 (1987); M. G. Rossmann, Proc. Natl. Acad. Sci. U.S.A. 85, 4625 (1988); P. Argos, EMBO J. 8, 779 (1989); J. P. M. Langedijk, J. J. Schalken, M. Tersmette, J. G. Huisman, R. H. Meloen, J. Gen. Virol. 71, 2609 (1990); V. Robert-Hebmann et al., Mol. Immunol. 29, 729 (1992).
    • (1992) Mol. Immunol. , vol.29 , pp. 729
    • Robert-Hebmann, V.1
  • 85
    • 0028019007 scopus 로고
    • S. Mathews et al., Nature 370, 666 (1994); M. Massiah et al., J. Mol. Biol. 244, 198 (1994); Z. Rao et al., Nature 378, 743 (1995); C. P. Hill, D. Worthylake, D. P. Bancroft, A. M. Christensen, W. I. Sundquist Proc. Natl. Acad. Sci. U.S.A. 93, 3099 (1996).
    • (1994) Nature , vol.370 , pp. 666
    • Mathews, S.1
  • 86
    • 0027987979 scopus 로고
    • S. Mathews et al., Nature 370, 666 (1994); M. Massiah et al., J. Mol. Biol. 244, 198 (1994); Z. Rao et al., Nature 378, 743 (1995); C. P. Hill, D. Worthylake, D. P. Bancroft, A. M. Christensen, W. I. Sundquist Proc. Natl. Acad. Sci. U.S.A. 93, 3099 (1996).
    • (1994) J. Mol. Biol. , vol.244 , pp. 198
    • Massiah, M.1
  • 87
    • 0029565831 scopus 로고
    • S. Mathews et al., Nature 370, 666 (1994); M. Massiah et al., J. Mol. Biol. 244, 198 (1994); Z. Rao et al., Nature 378, 743 (1995); C. P. Hill, D. Worthylake, D. P. Bancroft, A. M. Christensen, W. I. Sundquist Proc. Natl. Acad. Sci. U.S.A. 93, 3099 (1996).
    • (1995) Nature , vol.378 , pp. 743
    • Rao, Z.1
  • 91
    • 9444234724 scopus 로고    scopus 로고
    • note
    • 47-Hα.
  • 92
    • 0014413808 scopus 로고
    • P. B. Sigler, D. M. Blow, B. W. Mathews, R. Henderson, J. Mol. Biol. 35, 143 (1968); J. McConn, G. D. Fasman, G. P. Hess, ibid. 39, 551 (1969); S. T. Freer et al., Biochemistry 9, 1997 (1970); A. R. Fersht, J. Mol. Biol. 64, 497 (1972); J. Birktoft et al., Biochemistry 15, 4481 (1976); A. A. Kossiakoff et al., ibid. 16, 654 (1977); H. Felhammer et al., J. Mol. Biol. 111, 415 (1977); H. Huber and W. Bode, Acc. Chem. Res. 11, 114 (1978); L. Hedstrom et al., Biochemistry 35, 4515 (1996).
    • (1968) J. Mol. Biol. , vol.35 , pp. 143
    • Sigler, P.B.1    Blow, D.M.2    Mathews, B.W.3    Henderson, R.4
  • 93
    • 0014674111 scopus 로고
    • P. B. Sigler, D. M. Blow, B. W. Mathews, R. Henderson, J. Mol. Biol. 35, 143 (1968); J. McConn, G. D. Fasman, G. P. Hess, ibid. 39, 551 (1969); S. T. Freer et al., Biochemistry 9, 1997 (1970); A. R. Fersht, J. Mol. Biol. 64, 497 (1972); J. Birktoft et al., Biochemistry 15, 4481 (1976); A. A. Kossiakoff et al., ibid. 16, 654 (1977); H. Felhammer et al., J. Mol. Biol. 111, 415 (1977); H. Huber and W. Bode, Acc. Chem. Res. 11, 114 (1978); L. Hedstrom et al., Biochemistry 35, 4515 (1996).
    • (1969) J. Mol. Biol. , vol.39 , pp. 551
    • McConn, J.1    Fasman, G.D.2    Hess, G.P.3
  • 94
    • 0014965896 scopus 로고
    • P. B. Sigler, D. M. Blow, B. W. Mathews, R. Henderson, J. Mol. Biol. 35, 143 (1968); J. McConn, G. D. Fasman, G. P. Hess, ibid. 39, 551 (1969); S. T. Freer et al., Biochemistry 9, 1997 (1970); A. R. Fersht, J. Mol. Biol. 64, 497 (1972); J. Birktoft et al., Biochemistry 15, 4481 (1976); A. A. Kossiakoff et al., ibid. 16, 654 (1977); H. Felhammer et al., J. Mol. Biol. 111, 415 (1977); H. Huber and W. Bode, Acc. Chem. Res. 11, 114 (1978); L. Hedstrom et al., Biochemistry 35, 4515 (1996).
    • (1970) Biochemistry , vol.9 , pp. 1997
    • Freer, S.T.1
  • 95
    • 0015505502 scopus 로고
    • P. B. Sigler, D. M. Blow, B. W. Mathews, R. Henderson, J. Mol. Biol. 35, 143 (1968); J. McConn, G. D. Fasman, G. P. Hess, ibid. 39, 551 (1969); S. T. Freer et al., Biochemistry 9, 1997 (1970); A. R. Fersht, J. Mol. Biol. 64, 497 (1972); J. Birktoft et al., Biochemistry 15, 4481 (1976); A. A. Kossiakoff et al., ibid. 16, 654 (1977); H. Felhammer et al., J. Mol. Biol. 111, 415 (1977); H. Huber and W. Bode, Acc. Chem. Res. 11, 114 (1978); L. Hedstrom et al., Biochemistry 35, 4515 (1996).
    • (1972) J. Mol. Biol. , vol.64 , pp. 497
    • Fersht, A.R.1
  • 96
    • 0017119796 scopus 로고
    • P. B. Sigler, D. M. Blow, B. W. Mathews, R. Henderson, J. Mol. Biol. 35, 143 (1968); J. McConn, G. D. Fasman, G. P. Hess, ibid. 39, 551 (1969); S. T. Freer et al., Biochemistry 9, 1997 (1970); A. R. Fersht, J. Mol. Biol. 64, 497 (1972); J. Birktoft et al., Biochemistry 15, 4481 (1976); A. A. Kossiakoff et al., ibid. 16, 654 (1977); H. Felhammer et al., J. Mol. Biol. 111, 415 (1977); H. Huber and W. Bode, Acc. Chem. Res. 11, 114 (1978); L. Hedstrom et al., Biochemistry 35, 4515 (1996).
    • (1976) Biochemistry , vol.15 , pp. 4481
    • Birktoft, J.1
  • 97
    • 0017618454 scopus 로고
    • P. B. Sigler, D. M. Blow, B. W. Mathews, R. Henderson, J. Mol. Biol. 35, 143 (1968); J. McConn, G. D. Fasman, G. P. Hess, ibid. 39, 551 (1969); S. T. Freer et al., Biochemistry 9, 1997 (1970); A. R. Fersht, J. Mol. Biol. 64, 497 (1972); J. Birktoft et al., Biochemistry 15, 4481 (1976); A. A. Kossiakoff et al., ibid. 16, 654 (1977); H. Felhammer et al., J. Mol. Biol. 111, 415 (1977); H. Huber and W. Bode, Acc. Chem. Res. 11, 114 (1978); L. Hedstrom et al., Biochemistry 35, 4515 (1996).
    • (1977) Biochemistry , vol.16 , pp. 654
    • Kossiakoff, A.A.1
  • 98
    • 0017348682 scopus 로고
    • P. B. Sigler, D. M. Blow, B. W. Mathews, R. Henderson, J. Mol. Biol. 35, 143 (1968); J. McConn, G. D. Fasman, G. P. Hess, ibid. 39, 551 (1969); S. T. Freer et al., Biochemistry 9, 1997 (1970); A. R. Fersht, J. Mol. Biol. 64, 497 (1972); J. Birktoft et al., Biochemistry 15, 4481 (1976); A. A. Kossiakoff et al., ibid. 16, 654 (1977); H. Felhammer et al., J. Mol. Biol. 111, 415 (1977); H. Huber and W. Bode, Acc. Chem. Res. 11, 114 (1978); L. Hedstrom et al., Biochemistry 35, 4515 (1996).
    • (1977) J. Mol. Biol. , vol.111 , pp. 415
    • Felhammer, H.1
  • 99
    • 33947092515 scopus 로고
    • P. B. Sigler, D. M. Blow, B. W. Mathews, R. Henderson, J. Mol. Biol. 35, 143 (1968); J. McConn, G. D. Fasman, G. P. Hess, ibid. 39, 551 (1969); S. T. Freer et al., Biochemistry 9, 1997 (1970); A. R. Fersht, J. Mol. Biol. 64, 497 (1972); J. Birktoft et al., Biochemistry 15, 4481 (1976); A. A. Kossiakoff et al., ibid. 16, 654 (1977); H. Felhammer et al., J. Mol. Biol. 111, 415 (1977); H. Huber and W. Bode, Acc. Chem. Res. 11, 114 (1978); L. Hedstrom et al., Biochemistry 35, 4515 (1996).
    • (1978) Acc. Chem. Res. , vol.11 , pp. 114
    • Huber, H.1    Bode, W.2
  • 100
    • 0029863066 scopus 로고    scopus 로고
    • P. B. Sigler, D. M. Blow, B. W. Mathews, R. Henderson, J. Mol. Biol. 35, 143 (1968); J. McConn, G. D. Fasman, G. P. Hess, ibid. 39, 551 (1969); S. T. Freer et al., Biochemistry 9, 1997 (1970); A. R. Fersht, J. Mol. Biol. 64, 497 (1972); J. Birktoft et al., Biochemistry 15, 4481 (1976); A. A. Kossiakoff et al., ibid. 16, 654 (1977); H. Felhammer et al., J. Mol. Biol. 111, 415 (1977); H. Huber and W. Bode, Acc. Chem. Res. 11, 114 (1978); L. Hedstrom et al., Biochemistry 35, 4515 (1996).
    • (1996) Biochemistry , vol.35 , pp. 4515
    • Hedstrom, L.1
  • 104
    • 0030011638 scopus 로고    scopus 로고
    • in press
    • C. Aberham, S. Weber, W. Phares, J. Virol. 70, 3536 (1996); D. Braaten et al., J. Virol., in press.
    • J. Virol.
    • Braaten, D.1
  • 106
    • 9444254313 scopus 로고    scopus 로고
    • data not shown
    • R. K. Gitti et al., data not shown.
    • Gitti, R.K.1
  • 107
    • 9444242296 scopus 로고    scopus 로고
    • note
    • Supported by NIH grant AI30917 (M.F.S.), an award from the Searle Scholars Program (W.I.S.), a grant from the Lucille P. Markey Charitable Trust, and the University of Utah Cancer Center Support Grant (CA 42014). NMR instrumentation was purchased with partial support from NIH grant GM 42561. J.W. is supported by a Meyerhoff scholarship from the University of Maryland Baltimore County (UMBC). We are grateful to T. O'Hern (Howard Hughes Medical Institute, UMBC) and M. Zawrotny (UMBC) for technical support.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.