Exp Clin Endocrinol Diabetes 2005; 113(5): 245-247
DOI: 10.1055/s-2005-865679
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J. A. Barth Verlag in Georg Thieme Verlag KG Stuttgart · New York

Hormone Binding to the Follicle-Stimulating Hormone Receptor - Crystal Clear!

T. Gudermann1 , P. Nurwakagari1 , D. Ben-Menahem2
  • 1Institut für Pharmakologie und Toxikologie, Fachbereich Medizin, Philipps-Universität Marburg, Germany
  • 2Department of Clinical Pharmacology, Faculty of Health Sciences, Ben Gurion University of the Negev, Beer Sheba, Israel
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Publication History

Publication Date:
30 May 2005 (online)

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Abstract

The receptors for the trophic hormones luteinizing hormone (LH), follicle-stimulating hormone (FSH), and thyrotropin (TSH) play a central role in endocrinology. These receptors face the challenge to accommodate large heterodimeric glycoprotein ligands within their extracellular hormone-binding domain. Until recently, the mechanism of hormone binding and consequently the mode of receptor activation remained enigmatic. By solving the crystal structure of human follicle-stimulating hormone bound to the receptor's hormone binding domain, it has become clear that the follicle-stimulating hormone receptor grabs the glycoprotein hormone in a hand-clasp mode resulting in a hormone orientation perpendicular to the long axis of the ligand-binding domain. These findings have important ramifications for our understanding of the molecular mechanism of receptor activation and may provide a rational basis for the development of small, non-peptidic FSH receptor ligands.