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  • Title: Identification of amino acid residues 300-315 of the rat FSH receptor as a hormone binding domain: evidence for its interaction with specific regions of FSH beta-subunit.
    Author: Leng N, Dattatreyamurty B, Reichert LE.
    Journal: Biochem Biophys Res Commun; 1995 May 16; 210(2):392-9. PubMed ID: 7755615.
    Abstract:
    We previously reported that residues 9-30 of the extracellular N-terminus domain of the rat FSH receptor, which has no homologous sequence in receptors for related pituitary glycoprotein hormones, represented a specific FSH binding domain. Further examination of its deduced primary structure identified another region, residues 300-315, which was also unique to the FSH receptor. To determine whether this region of the FSH receptor was involved in hormone binding, a synthetic peptide corresponding to residues 300-315 was studied with respect to its ability to bind FSH, as well as a series of nine overlapping synthetic peptides corresponding to the entire primary structure of the hormone specific FSH beta-subunit. 125I-FSH rec-(300-315) peptide bound to immobilized human, ovine and bovine FSH, but not to prolactin or ovalbumin. Of the nine synthetic peptides studied, binding was restricted to FSH beta residues 21-35, and to a much lesser extent (20%) to residues 11-25. All binding was abolished in the presence of excess solubilized FSH receptor. Earlier studies indicated that although FSH binds to FSH rec(9-30) peptide, residues 11-25 or 21-35 of the FSH beta-subunit were not involved. Our results suggest the FSH receptor N-terminus, extracellular residues 300-315, may define a FSH binding site, and that binding of FSH beta-subunit may occur via interactions with FSH beta 21-35 and 11-25.
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