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Relationships among several different non-homologous polypeptide hormones

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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.

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  1. Department of Biochemistry, McMaster University Health Sciences Centre, 1200 Main Street West, L8N 3Z5, Hamilton, Ontario, Canada

    Richard M. Epand

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Epand, R.M. Relationships among several different non-homologous polypeptide hormones. Mol Cell Biochem 57, 41–47 (1983). https://doi.org/10.1007/BF00223523

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  • DOI: https://doi.org/10.1007/BF00223523

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