Ligand binding to wild-type and E-B13Q mutant insulins: A three-state allosteric model system showing half-site reactivity

Journal of Molecular Biology

Volumn 245, Issue 4, 1995, Pages 324-330

  Bloom, Curtis R ^a   Choi, Wonjae E ^a   Brzovic, Peter S ^a,b   Ha, Julie J ^d   Huang, Sheng Tung ^a   Kaarsholm, Niels C ^c   Dunn, Michael F ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

^c Novo Research Institute   (Denmark)

^d NONE

Author keywords

Allostery; Cooperativity; Half site; Insulin

Indexed keywords

EID: 0028940094     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1994.0027     Document Type: Editorial

References (24)

1. Baker, E. N., Blundell, T. L., Cutfield, J. F., Cutfield, S. M., Dodson, E. J., Dodson, G. G., Hodgkin, D. C., Hubbard, R. E., Isaacs, N. W., Reynolds, C. D., Sakabe, K., Sakabe, N. & Vijayan, N. M. (1988). The structure of 2Zn pig insulin crystals at 1.5 A resolution. Phil. Trans. Roy. Soc. ser. B, 319, 369-456.
2. Bentley G. A., Brange, J., Dereweneda, Z., Dodson, E. J., Dodson, G. G., Markussen, J., Wilkinson, A. J., Wollmer, A. & Xaio, B. (1992). Role of B13 Glu in insulin assembly (the hexamer structure of recombinant B13 glu-gln) insulin. J. Mol Biol. 228, 1163-1176.
3. Brader, M. L. & Dunn, M. F. (1991). Insulin hexamers: new conformations and applications. Trends Biochem. Sci. 16, 341-345.
4. Brader, M. L., Kaarsholm, N. C., Lee, W.-K. & Dunn, M. F. (1991). Characterization of the R-state insulin hexamer and its derivatives. The hexamer is stabilized by heterotropic ligand binding interactions. Biochemistry, 30, 6636-6645.
5. Brzovic, P. S., Choi, W. E., Borchardt, D., Kaarsholm, N. C. & Dunn, M. F. (1994). Structural asymmetry and half-site reactivity in the T- to R-allosteric transition of the insulin hexamer. Biochemistry, 33, 13057-13069.
6. Choi, W. E., Brader, M. L., Aguilar, V., Kaarsholm, N. C. & Dunn, M. F. (1993). The allosteric transition of the insulin hexamer is modulated by homotropic and heterotropic interactions. Biochemistry, 32, 11638-11645.
7. Ciszak, E. & Smith, G. D. (1994). Crystallographic evidence for dual coordination around zinc in the T3R3 human insulin hexamer. Biochemistry, 33, 1512-1517.
8. Derewenda, U., Derewenda, Z., Dodson, E. J., Dodson, G. G., Reynolds, C. D., Smith, G. D., Sparks, C. & Swensen, D. (1989). Phenol stabilizes more helix in a new symmetrical Zn insulin hexamer. Nature (London), 338, 594-596.
9. 2 + in the assembly and storage of the insulin hexamer. Biochemistry, 30, 917-924.
10. Kaarsholm, N. C., Ko, H.-C. & Dunn, M. F. (1989). Comparison of solution structural flexibility and zinc binding domains for insulin, pro-insulin, and minipro insulin. Biochemistry, 28, 4427-4435.
11. Kaarsholm, N. C., Havelund, S. & Hougaard, P. (1990). Ionization of native and mutant insulins: pK perturbation of B13-glu in aggregated species. Arch. Biochem. Biophys. 283, 496-502.
12. Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
13. Koshland, D. E., Nemethy G. & Filmer, D. (1966). Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry, 5, 365-385.
14. Markussen, J., Diers, I., Engesgaard, A., Hansen, M. T., Hougaard, P., Langkjaer, L., Norris, K., Ribel, U., Sorensen, A. R., Sorensen, E. & Voigt, H. O. (1987). Soluble, prolonged-acting insulin derivatives. II. Degree of proaction and crystallizability of insulins substituted in positions A17, B8, B13, B27, and B30. Protein Eng. 1, 215-223.
15. Matthews, B. & Bernhard, S. A. (1973). Structure and symmetry of oligomeric enzymes. Annu. Rev. Biophys. Bioeng. 2, 215-317.
16. Monod, J., Wyman, J. & Changeux, J.-P. (1965). On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88-118.
17. Perutz, M. F. (1989). Mechanisms of cooperativity and allosteric regulation in proteins. Quart. Rev. Biophys. 22, 139-237.
18. Porter, R. R. (1953). Partition chromatography of insulin and other proteins. Biochem. J. 53, 320-328.
19. Roy M., Brader, M. L., Lee, R. W.-K., Kaarsholm, N. C., Hansen, J. & Dunn, M. F. (1989). Spectroscopic signatures of the T- to R-conformational transition in the insulin hexamer. J. Biol. Chem. 264, 19081-19085.
20. Seydoux, F., Malhotra, O. P. & Bernhard, S. A. (1974). Half-site reactivity CRC Crit. Rev. Biochem. 2, 227 -257.
21. Smith, G. D. & Dodson, G. G. (1992a). The structure of a rhombohedral R6 insulin hexamer that binds phenol. Biopolymers, 32, 1749-1756.
22. Smith, G. D. & Dodson, G. G. (1992b). Structure of a rhombohedral R6 insulin-phenol complex. Proteins: Struct. Func. Genet. 14, 401-408.
23. Steiner, D. F. (1976). Insulin today Diabetes, 26, 322-340.
24. Sudmeier, J. L., Bell, S. J., Storm, M. C. & Dunn, M. F. (1981). Cadmium-113 NMR studies of bovine insulin; the two zinc insulin hexamer specifically binds calcium ion. Science, 212, 560-562.