Abstract
The determination of the structure of the insulin hexamer has made it possible to design amino acid substitutions which alter insulin’s activity and association properties. This has given insight into insulin’s biological function and has led to improvement in clinical preparations of insulin.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Adams M.J., Blundell T.L., Dodson E.J., Dodson G.G., Vijayan M., Baker E.N., Harding M.M., Hodgkin D.C., Rimmer B. and Sheat S. “Structure of rhombohedral 2 zinc insulin crystals.” Nature 224 (1969): 491–495.
Baker E.N., Blundell T.L., Cutfield J.F., Cutfield S.M., Dodson E.J., Dodson G.G., Crowfoot D.M., Hodgkin D.C., Hubbard R.E., Isaacs N.W., Reynolds C.D., Sakabe K., Sakabe N. and Vijayan N.M. “The structure of 2Zn pig insulin crystals at 1.5 Å resolution.” Philosophical Transactions of the Royal Society of London 319 (1988): 371–456.
Bentley G., Dodson E., Dodson G., Hodgkin D. and Mercola D. “Structure of insulin in 4-zinc insulin.” Nature 261 (1976): 166–168.
Bentley G.A., Brange J., Derewenda Z., Dodson E.J., Dodson G.G., Markussen J., Wilkinson A.J., Wollmer A. and Xiao B. “Role of B13 in insulin assembly. The hexamer structure of recombinant mutant (B13 Glu to Gln) insulin.” Journal of. Molecular Biology 228 (1992): 1163–1176.
Brange J., Ribel U., Hansen J.F., Dodson G., Hansen M.T., Havelund S., Melberg S.G., Norris F., Norris K., Snel L., Sørensen A.R. and Voigt H.O. “Monomeric insulins obtained by protein engineering and their medical implications.” Nature 333 (1988): 679–682.
Brown H., Sanger F. and Kitai R. “The Structure of Pig and Sheep Insulin.” Biochemistry Journal 60 (1955): 556–565.
Derewenda U., Derewenda Z., Dodson E.J., Dodson G.G., Reynolds C.D., Smith G.D., Sparks C. and Swenson D. “Phenol stabilizes more helix in a new symmetrical zinc insulin hexamer.” Nature 338 (1989): 594–596.
Dodson E.J., Dodson G.G., Hubbard R.E., Moody P.C.E., Turkenburg J., Whittingham J., Xiao B., Brange J., Kaarsholm N. and Thogersen H. “Insulin assembly: its modification by protein engineering and ligand binding.” Philosophical Transactions of the Royal Society, London A 345 (1993): 153–164.
Kraulis P.J. “MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures.” Journal of Applied Crystallography 24 (1991): 946–950.
Renscheidt H., Strassburger W., Glatter U., Wollmer A., Dodson G.G. and Mercola D.A. “A solution equivalent of the 2Zn → 4Zn transformation of insulin in the crystal.” European Journal of Biochemistry 142 (1984): 7–14.
Steiner D.F. and Oyer P.E. “The biosynthesis of insulin and probable precursor of insulin by a human islet cell adenoma.” Proceedings of the National Academy of Sciences USA 57 (1967): 473–480.
Whittingham J.L., Edwards D.J., Antson A.A., Clarkson J.M. and Dodson G.G. “Interactions of Phenol and m-Cresol in the Insulin Hexamer, and their Effect on the Association Properties of B28 Pro → Asp Insulin Analogues.” Biochemistry 37 (1998): 11516–11523.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Kluwer Academic Publishers
About this chapter
Cite this chapter
Dodson, G.G., Whittingham, J.L. (2002). Insulin: Sequence, Structure and Function - A Story of Surprises. In: Dieken, M.L., Federwisch, M., De Meyts, P. (eds) Insulin & Related Proteins - Structure to Function and Pharmacology. Springer, Dordrecht. https://doi.org/10.1007/0-306-47582-0_3
Download citation
DOI: https://doi.org/10.1007/0-306-47582-0_3
Publisher Name: Springer, Dordrecht
Print ISBN: 978-1-4020-0655-5
Online ISBN: 978-0-306-47582-5
eBook Packages: Springer Book Archive