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Principles of protein–protein recognition

Naturevolume 256pages705708 (1975) | Download Citation

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Abstract

The formation of the protein–protein interface by the insulin dimer, the trypsin-PTI complex and the αβ oxyhaemoghbin dimer removes 1,130–1,720 Å2 of accessible surface from contact with water. The residues forming the interface are close packed: each occupies the same volume as it does in crystals of amino acids. These results indicate that hydrophobicity is the major factor stabilising protein–protein association, while complementarity plays a selective role in deciding which proteins may associate.

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References

  1. 1

    Blundell, T., Dodson, G., Hodgkin, D., and Mercola, D., Adv. Protein Chem., 26, 279–402 (1972).

  2. 2

    Huber, R., Kukla, D., Bode, W., Schwager, P., Bartels, K., Deisenhofer, J., and Steigemann, W., J. molec. Biol., 89, 73–101 (1974).

  3. 3

    Rühlmann, A., Kukla, D., Schwager, P., Bartels, K., and Huber, R., J. molec. Biol., 77, 417–436 (1973).

  4. 4

    Perutz, M. F., Muirhead, H., Cox, J. M., and Goaman, L. C. G., Nature, 219, 131 (1968).

  5. 5

    Lee, B., and Richards, F. M., J. molec. Biol., 55, 379–400 (1971).

  6. 6

    Chothia, C. H., Nature, 248, 338–339 (1974).

  7. 7

    Chothia, C. H., Nature, 254, 304–308 (1975).

  8. 8

    Deisenhofer, M., and Steigemann, W., Second Int. Res. Conf. Proteinase Inhibitors, (Springer, Heidelberg, 1974).

  9. 9

    Richards, F. M., J. molec. Biol., 82, 1–14 (1974).

  10. 10

    Doty, P., and Myers, G. E., Discussion Faraday Soc., 13, 51 (1953).

  11. 11

    Page, M. I., and Jencks, W. P., Proc. natn. Acad. Sci. U.S.A., 68, 1678–1683 (1971).

  12. 12

    Pekar, A. H., and Frank, B. H., Biochemistry, 11, 4013–4016 (1972).

  13. 13

    Vincent, J. P., and Lazdunski, M., Biochemistry, 11, 2967–2977 (1972).

  14. 14

    Kellett, G. L., and Schachman, H. K., J. molec. Biol., 59, 387–399 (1971).

  15. 15

    Pauling, L., and Pressman, D., J. Am. chem. Soc., 67, 1003–1012 (1945).

  16. 16

    Kauzmann, W., Adv. Protein Chem., 14, 1–63 (1959).

  17. 17

    Schellman, J. A., C.r. Trav. Lab. Carlsberg, Serv. Chim., 29, 223–229 (1955).

  18. 18

    Klotz, I. M., and Franzen, J. S., J. Am. chem. Soc., 84, 3461–3466 (1962).

  19. 19

    Kresheck, G. C., and Klotz, I. M., Biochemistry, 8, 8–12 (1969).

  20. 20

    Maitland, G. C., and Smith, B. B., Chem. Soc. Rev., 2, 181–210 (1973).

  21. 21

    Hermann, R. B., J. phys. Chem., Ithaca, 76, 2754 (1972).

  22. 22

    Reynolds, J. A., Gilbert, D. B., and Tanford, C., Proc. natn. Acad. Sci. U.S.A., 71, 2925–2927 (1974).

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  1. Service de Biochimie Cellulaire, Institut Pasteur, 75015, Paris, France

    • Cyrus Chothia
    •  & Joël Janin

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https://doi.org/10.1038/256705a0

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