Abstract
Follicle-stimulating hormone receptor (FSHR) is a glycoprotein hormone receptor and possesses a large extracellular domain (ECD) instrumental in hormone binding. The ECD is characterized by the presence of leucine-rich repeat (LRR) structures made up of alpha-helices flanked by beta-strands. Our previous studies with the synthetic peptides corresponding to the potentially surface-oriented regions of the ECD had led to the identification of some of these regions in either FSH-binding or FSH-induced cAMP production or both. This study was undertaken with an aim to correlate the findings made in vitro with the secondary structures of the respective peptides. Accordingly, all peptides were screened for their secondary structures in different biochemical environments. This study correlates the observed alpha-helical signature with the previously demonstrated activity in signal generation for peptides 15-31 and 216-235 hFSHR, while FSH binding is correlated with the maintenance of beta-sheet structure in peptides 285-300 and 297-310 hFSHR as observed in vitro.
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