title: Symmetrical features in polypeptide hormone-receptor interactions.
abstract: Symmetrical features were observed in the amino acid sequences of some biologically active peptides. It is suggested that this approximate symmetry is reflected in the conformations of the peptides at their respective biological receptors, and has arisen by natural selection as both peptides and receptors evolved to optimise their mutual fit. It follows that the binding site for each peptide at its receptor would share the same symmetry element. This would arise if the peptide binds to two symmetrically related similar or identical submits in the receptor.
mesh_terms: D000595:Amino Acid Sequence; D000804:Angiotensin II; D001665:Binding Sites; D001920:Bradykinin; D005934:Glucagon; D007987:Gonadotropin-Releasing Hormone; D008968:Molecular Conformation; D010455:Peptides; D011487:Protein Conformation; D011956:Receptors, Cell Surface; D013973:Thyrotropin-Releasing Hormone
chemical_list: D010455:Peptides; D011956:Receptors, Cell Surface; D000804:Angiotensin II; D007987:Gonadotropin-Releasing Hormone; D013973:Thyrotropin-Releasing Hormone; D005934:Glucagon; D001920:Bradykinin