Minimal steric difference study of structural requirements for the luteinizing hormone-releasing hormone (LH-RH) receptor.

Quantitative structure-activity relation for amino acid substitution analogues of the LH-RH decapeptide were established by means of the receptor site mapping procedure based upon minimal steric differences. For a series of 17 analogues of LH-RH, obtained by substitutions of the C-terminal Gly-NH2 residue, a corelation coefficient r = 0.93 was obtained, for a series of 7 analogues, obtained by substitutions of the Leu7 residue, r = 0.95 was obtained. The shape of the LH-RH receptor regions interacting with the C-terminal of the decapetide and with the Leu7-side chain is inferred from this study.