[Identification of an active site in luteotropin (LH) and chorionic gonadotropin (CG) based on studies of their conformation in solution by proton nuclear magnetic resonance (NMR) and on the receptor-binding properties of hormone fragments].
Using porcine LH, the presence of a site of interaction with the specific testicular receptor of these hormones was demonstrated in the carboxyterminal part of the alpha subunit. This conclusion is based on results of studies of chemical mutilations and conformation in solution of these hormones and of their subunits by NMR. A NMR study of human CG showed that this was also applicable to this hormone. The synthetic peptide Tyr-Tyr-His-Lys-Ser, which corresponds to the carboxyterminal part of the alpha subunit does not demonstrate high affinity for binding to the receptor. These findings indicate that the formation of one of the active sites of these gonadotropins depends necessarily on their quaternary structure. The peptide corresponding to the site of uptake must be bound within the hormonal alpha beta complex to enable effective interaction with the receptor.
D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D006063:Chorionic Gonadotropin; D006801:Humans; D007700:Kinetics; D007986:Luteinizing Hormone; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011956:Receptors, Cell Surface; D011974:Receptors, LH; D013552:Swine
D006063:Chorionic Gonadotropin; D011956:Receptors, Cell Surface; D011974:Receptors, LH; D007986:Luteinizing Hormone
Identification d'un site actif dans la lutropine (LH) et la choriogonadotropine (CG) basée sur l'étude de leur conformation en solution par résonance magnétique nucléaire (RMN) du proton et sur les propriétés de liaison au récepteur de fragments d'hormone.