[Original hypothesis on the specificity of the binding of glycoprotein hormones to their receptors].
From the data we have obtained in the last few years concerning the interaction of gonadotropins with their receptors in vitro we develop a coherent model of the mechanism responsible for the binding specificity of these hormones. In this model we postulate that there is structural separation between the sites responsible for the high affinity of this class of hormones for their receptors and the sites responsible for the specificity of binding of these hormones. The high affinity site would be common to all the glycoprotein hormones and would be mainly formed by the alpha subunit which is common to all these hormones. The specific sites would act by inhibiting the binding of each hormone to the receptors of the others. These sites would be borne mainly by the specific beta subunits. We have introduced the term "negative specificity" to describe this mechanism.
D000818:Animals; D005640:Follicle Stimulating Hormone / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism*; D006064:Gonadotropins, Equine / Q000378:metabolism; D006736:Horses; D066298:In Vitro Techniques; D007986:Luteinizing Hormone / Q000378:metabolism; D010907:Pituitary Hormones / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D013552:Swine
D006023:Glycoproteins; D006064:Gonadotropins, Equine; D010907:Pituitary Hormones; D011956:Receptors, Cell Surface; D007986:Luteinizing Hormone; D005640:Follicle Stimulating Hormone
Hypothèse originale sur la spécificité de liaison des hormones glycoprotéiques à leurs récepteurs.