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Structural patterns in globular proteins

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Abstract

A simple diagrammatic representation has been used to show the arrangement of α helices and β sheets in 31 globular proteins, which are classified into four clearly separated classes. The observed arrangements are significantly non-random in that pieces of secondary structure adjacent in sequence along the polypeptide chain are also often in contact in three dimensions.

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References

  1. Schulz, G. E., and Schirmer, R. H., Nature, 250, 144–145 (1974).

    ADS  Google Scholar 

  2. Rossman, M. G., Moras, D., and Olsen, K. W., Nature, 250, 194–199 (1974).

    ADS  Google Scholar 

  3. Hendrickson, W. A., Klipperstein, G. L., and Ward, K. B., Proc. natn. Acad. Sci. U.S.A., 72, 2160–2164 (1975).

    ADS  CAS  Google Scholar 

  4. Kretsinger, R. H., and Nuckolds, C. E., J. biol. Chem., 248, 3313–3326 (1973).

    CAS  PubMed  Google Scholar 

  5. Kendrew, J. C., Dickerson, R. E., Strandberg, B. E., Hart, R. G., and Davies, D. R., Nature, 185, 422–425 (1960).

    ADS  CAS  PubMed  Google Scholar 

  6. Watson, H. C., in Prog. Stereochem., 4, 299–333 (1960).

    Google Scholar 

  7. Watenpaugh, K. D., Sieker, L. C., Herriott, J. R., and Jensen, L. H., Acta Crystallogr., B 29, 943–956 (1973).

    CAS  Google Scholar 

  8. Schiffer, M., Girling, R. L., Ely, K. R., and Edmundson, A. B., Biochemistry, 12, 4620–4631 (1973).

    CAS  PubMed  Google Scholar 

  9. Poljak, R. J., et al., Proc. natn. Acad. Sci. U.S.A., 70, 3305–3310 (1973).

    ADS  CAS  Google Scholar 

  10. Segal, D. M., et al., Proc. natn. Acad. Sci. U.S.A., 71, 4298–4302 (1974).

    ADS  CAS  Google Scholar 

  11. Epp, C., et al., Eur. J. Biochem., 45, 513–524 (1974).

    CAS  PubMed  Google Scholar 

  12. Blake, C. C. F., Geisow, M. J., Swan, I. D. A., Rerat, C., and Rerat, B., J. molec. Biol., 88, 1–12 (1974).

    CAS  PubMed  Google Scholar 

  13. Richardson, J. S., Thomas, K. A., Rubin, B. H., and Richardson, D. C., Proc. natn. Acad. Sci. U.S.A., 72, 1349–1353 (1975).

    ADS  CAS  Google Scholar 

  14. Edelman, G. M., et al., Proc. natn. Acad. Sci. U.S.A., 69, 2580–2584 (1972).

    ADS  CAS  Google Scholar 

  15. Hardman, K. D., and Ainsworth, C. F., Biochemistry, 11, 4910–4919 (1972).

    CAS  PubMed  Google Scholar 

  16. Birktoft, J. J., Blow, D. M., Henderson, R., and Steitz, T. A., Proc. R. Soc., B 257, 67–76 (1970).

    CAS  Google Scholar 

  17. Birktoft, J. J., and Blow, D. M., J. molec. Biol., 68, 187–240 (1972).

    CAS  PubMed  Google Scholar 

  18. Adams, M. J., et al., Nature, 224, 491–495 (1969).

    ADS  CAS  Google Scholar 

  19. Huber, R., Kukla, D., Ruhlmann, A., and Steigemann, W., in Proc. Int. Res. Conf. Proteinase Inhibitors, Munich 1970 (edit. by Fritz, H., and Tschesche, H.), 56–64 (de Gruyter, Berlin, 1970).

    Google Scholar 

  20. Mathews, F. S., Levine, M., and Argos, P., Nature new Biol., 233, 15–16 (1971).

    ADS  CAS  PubMed  Google Scholar 

  21. Wyckoff, H. W., et al., J. biol. Chem., 245, 305–328 (1970).

    CAS  PubMed  Google Scholar 

  22. Blake, C. C. F., Mair, G. A., North, A. C. T., Phillips, D. C., and Sarma, V. R., Proc. R. Soc., B 167, 365–385 (1967).

    ADS  CAS  Google Scholar 

  23. Arnone, A., et al., J. biol. Chem., 246, 2302–2316 (1971).

    CAS  PubMed  Google Scholar 

  24. Matthews, B. W., and Remington, S. J., Proc. natn. Acad. Sci. U.S.A., 71, 4178–4182 (1975).

    ADS  Google Scholar 

  25. Drenth, J., Jansonius, J. M., Koekoek, R., and Wolthers, B. G., Adv. Protein Chem., 25, 79–115 (1971).

    CAS  PubMed  Google Scholar 

  26. Colman, P. M., Jansonius, J. N., and Matthews, B. W., J. molec. Biol., 70, 701–724 (1972).

    CAS  PubMed  Google Scholar 

  27. Holmgren, A., Soderberg, B. -O., Elkund, H., and Branden, C. -I., Proc. natn. Acad. Sci. U.S.A., 72, 2307–2309 (1975).

    ADS  Google Scholar 

  28. Watenpaugh, K. D., Sieker, L. C., Jensen, L. H., Legall, J., and Dubourdieu, M., Proc. natn. Acad. Sci. U.S.A., 69. 3185–3188 (1972).

    ADS  CAS  Google Scholar 

  29. Anderson, R. D., Proc. natn. Acad. Sci. U.S.A., 69, 3189–3191 (1972).

    ADS  Google Scholar 

  30. Branden, C. I., et al., Proc. natn. Acad. Sci. U.S.A., 70, 2439–2442 (1973).

    ADS  CAS  Google Scholar 

  31. Campbell, J. W., Watson, H. C., and Hodgson, G. I., Nature, 250, 301–303 (1974).

    ADS  CAS  PubMed  Google Scholar 

  32. Schulz, G. E., Elzinga, M., Marx, F., and Schirmer, R. H., Nature, 250, 120–123 (1974).

    ADS  CAS  PubMed  Google Scholar 

  33. Banner, D. W., et al., Nature, 255, 609–614 (1975).

    ADS  CAS  PubMed  Google Scholar 

  34. Wright, C. S., Alden, R. A., and Kraut, J., Nature, 221, 235–242 (1969).

    ADS  CAS  PubMed  Google Scholar 

  35. Quiocho, F. A., and Lipscomb, W. N., Adv. Protein Chem., 25, 1–78 (1971).

    CAS  PubMed  Google Scholar 

  36. Adams, M. J., Ford, G. C., Liljas, A., and Rossmann, M. G., Biochem. biophys. Res. Commun., 53, 46–51 (1973).

    CAS  PubMed  Google Scholar 

  37. Blake, C. C. F., and Evans, P. R., J. molec. Biol., 84, 585–603 (1974).

    CAS  PubMed  Google Scholar 

  38. Blake, C. C. F., in Essays in Biochemistry, 11, 37–79 (edit. by Campbell, P. N. and Aldridge, W. N.) (Academic, London 1975).

  39. Buehner, M., Ford, G. C., Moras, D., Olsen, K. W., and Rossmann, M. G., Proc. natn. Acad. Sci. U.S.A., 70, 3052–3054 (1973).

    Google Scholar 

  40. Fletterick, R. J., Bates, D. J., and Steitz, T. A., Proc. natn. Acad. Sci. U.S.A., 72, 38–42 (1975).

    ADS  CAS  Google Scholar 

  41. Stroud, R. M., Kay, L. M., and Dickerson, R. E., J. molec. Biol., 83, 185–208 (1974).

    CAS  PubMed  Google Scholar 

  42. Shotton, D. M., and Watson, H. C., Nature, 225, 811–816 (1970).

    ADS  CAS  PubMed  Google Scholar 

  43. Perutz, M. F., et al., Nature, 222, 1240–1244 (1968).

    ADS  Google Scholar 

  44. Baldwin, J. M., prog. Biophys. molec. Biol., 29, 225–320 (1975).

    CAS  Google Scholar 

  45. Carter, C. W., Jr, et al., J. biol. Chem., 249, 4212–4225 (1974).

    CAS  PubMed  Google Scholar 

  46. Salemme, F. R., et al., J. biol. Chem., 248, 3910–3921 (1973).

    CAS  PubMed  Google Scholar 

  47. Hill, E., Tsernoglou, Webb, L., and Banaszak, L. J., J. molec. Biol., 72, 577–591 (1972).

    CAS  PubMed  Google Scholar 

  48. Adman, E. T., Sieker, L. C., and Jensen, L. H., J. biol. Chem., 248, 3987–3996 (1973).

    CAS  PubMed  Google Scholar 

  49. Bergsma, J., et al., J. molec. Biol., 98, 637–643 (1965).

    Google Scholar 

  50. Kannan, K. K., et al., Cold Spring Harb. Symp. quant. Biol., 36, 221–231 (1971).

    CAS  Google Scholar 

  51. Sweet, R. M., Wright, H. T., Chothia, C. H., and Blow, D. M., Biochemistry, 13, 4213–4228 (1974).

    Google Scholar 

  52. Champness, J. N., et al., Nature, 259, 20–24 (1976).

    ADS  CAS  PubMed  Google Scholar 

  53. Holmes, K. C., Stubbs, G. J., Mandelkow, E., and Gallwitz, U., Nature, 254, 192–196 (1975).

    ADS  CAS  PubMed  Google Scholar 

  54. Henderson, R., and Unwin, P. N. T., Nature, 257, 28–32 (1975).

    ADS  CAS  Google Scholar 

  55. Rao, S. T., and Rossmann, M. G., J. molec. Biol., 76, 241–256 (1973).

    CAS  PubMed  Google Scholar 

  56. Karplus, M., and Weaver, D. L., Nature, 260, 404–406 (1976); Sternberg, M. J. E., and Thornton, J. M., J. molec. Biol. (in the press).

    ADS  CAS  PubMed  Google Scholar 

  57. Richardson, J. S., Richardson, D. C., Thomas, K. A., Silverton, E. W., and Davies, D. R., J. molec. Biol., 102, 221–235 (1976).

    CAS  PubMed  Google Scholar 

  58. Phillips, D. C., Proc. natn. Acad. Sci. U.S.A., 57, 484–495 (1967).

    ADS  CAS  Google Scholar 

  59. Goldberg, M. E., J. molec. Biol., 46, 441–446 (1969).

    CAS  PubMed  Google Scholar 

  60. Veron, M., Falcoz-Kelly, F., and Cohen, G. N., Eur. J. Biochem., 28, 520–527 (1972).

    CAS  PubMed  Google Scholar 

  61. Light, A., Taniuchi, H., and Chen, R. F., J. biol. Chem., 249, 2285–2299 (1974).

    CAS  PubMed  Google Scholar 

  62. Ptitsyn, O. B., and Rashin, A. A., Biophys. Chem., 3, 1–20 (1974).

    Google Scholar 

  63. Wetlaufer, D. E., Proc. natn. Acad. Sci. U.S.A., 70, 697–701 (1974).

    ADS  Google Scholar 

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Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Michael Levitt

  2. Service de Biochemie Cellulaire, Institut Pasteur, 75724, Paris, France

    Cyrus Chothia

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  1. Michael Levitt
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  2. Cyrus Chothia
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Levitt, M., Chothia, C. Structural patterns in globular proteins. Nature 261, 552–558 (1976). https://doi.org/10.1038/261552a0

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