Add time:08/09/2019         Source:sciencedirect.com

We have recently identified a region, N-terminus residues 9–30, in the extracellular domain of the follicle-stimulating hormone (FSH) receptor capable of binding FSH, but not luteinizing hormone (LH) or thyroid-stimulating hormone (FSH) (Dattatreyamurty and Reichert (1992) Mol. Cell. Endocrinol. 87, 9–17). The objectives of the present study were to examine the interaction between a synthetic peptide corresponding to this receptor sequence and the β-subunit of FSH, and to identify which FSH-β regions are involved in the interaction. FSH-β subunit and synthetic FSH-β peptides 1–15, 71–85 and 101–111 effectively bound 125I-labeled FSH rec-(9–30) peptide, and binding was inhibited by excess unlabeled FSH receptors. Scatchard analysis indicated that the synthetic FSH-β peptides had affinities for FSH rec-(9–30) peptide in the order of 106 M−1 (Ka), with the sum of individual peptide affinities (Ka = 1.21 × 107 M−1) closely approximating that of the intact β-subunit (1.02 × 107 M−1). Polyclonal antibodies raised against FSH rec-(9–30) peptide completely inhibited the binding of 125I-labeled receptor peptide to hFSH, hFSH-β, and hFSH-β peptides 1–15, 71–85 and 101–111. Our results indicate that recognition of FSH-β by N-terminus region (9–30) of the FSH receptor involves contact with residues in three discontinuous binding regions on FSH-β. The latter finding suggests that these three discontinuous sequence regions of FSH-β may be closely oriented on the hormone surface to form a contiguous region in the three-dimensional structure required for recognition by the N-terminus region (residues 9–30) of the FSH receptor.

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