Hormone binding to the follicle-stimulating hormone receptor - Crystal clear!

T. Gudermann, P. Nurwakagari, D. Ben-Menahem

Research output: Contribution to journalShort surveypeer-review

2 Scopus citations

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.

Original languageEnglish
Pages (from-to)245-247
Number of pages3
JournalExperimental and Clinical Endocrinology and Diabetes
Volume113
Issue number5
DOIs
StatePublished - 1 May 2005

Keywords

  • Crystal structure
  • Follicle-stimulating hormone
  • G proteins
  • Glycoprotein hormones

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