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Symmetrical features in polypeptide hormone-receptor interactions.

C R Beddell, G C Sheppey, T L Blundell

    International Journal of Peptide and Protein Research
    |January 1, 1977
    PubMed
    Summary

    Biologically active peptides exhibit symmetrical amino acid sequences. This symmetry suggests a co-evolutionary process with receptors, optimizing molecular interactions and binding sites for enhanced biological function.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Evolutionary Biology

    Background:

    • Symmetrical features are present in the amino acid sequences of certain biologically active peptides.
    • This observed symmetry may extend to the three-dimensional conformations of these peptides when interacting with their biological receptors.

    Purpose of the Study:

    • To investigate the hypothesis that the symmetry in peptide sequences is a result of natural selection.
    • To explore the implications of peptide-receptor symmetry for optimizing mutual fit and binding interactions.

    Main Methods:

    • Analysis of amino acid sequences of biologically active peptides to identify symmetrical patterns.
    • Theoretical modeling and comparative analysis of peptide-receptor interactions based on symmetry principles.

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    Main Results:

    • Approximate symmetry in amino acid sequences of biologically active peptides was confirmed.
    • A correlation was proposed between peptide sequence symmetry and conformational symmetry at the receptor binding site.

    Conclusions:

    • The observed peptide symmetry likely evolved via natural selection to enhance the precise fit between peptides and their receptors.
    • The binding site at the receptor is hypothesized to possess symmetry, potentially involving two symmetrically related receptor subunits for peptide binding.