Molecular and Cellular Biochemistry

, Volume 57, Issue 1, pp 41–47

Relationships among several different non-homologous polypeptide hormones

Authors

  • Richard M. Epand
    • Department of BiochemistryMcMaster University Health Sciences Centre
Article

DOI: 10.1007/BF00223523

Cite this article as:
Epand, R.M. Mol Cell Biochem (1983) 57: 41. doi:10.1007/BF00223523

Summary

Several polypeptide hormones of apparently diverse structure and function have a number of similarities which suggest that there may be common features in their mechanism of action. These hormones are all composed of a single linear sequence of about 30 amino acids; their hydrophobic amino acids are regularly spaced at every third or fourth amino acid residue, allowing them to form amphipathic structures which can interact with phospholipids; a fragment at or near their N-terminus is required for biological activity. These hormones include glucagon, β-endorphin, parathyroid hormone and calcitonin. A model is proposed in which all regions of the hormone bind to the receptor with comparable affinity except for a small segment which, when intact, triggers a conformational change in the receptor resulting in a further stabilization of the hormone-receptor complex. The activity of partial sequences and chemically modified forms of β-endorphin, parathyroid hormone and glucagon are discussed in relation to this model.

Copyright information

© Martinus Nijhoff Publishers 1983