The specificity of binding of glycoprotein hormones to their receptors

G. Caltabiano, M. Campillo, A. De Leener, G. Smits, G. Vassart, S. Costagliola, L. Pardo

Research output: Contribution to journalReview articleResearchpeer-review

43 Citations (Scopus)

Abstract

The glycoprotein hormone receptor family is peculiar because, in contrast to other G protein-coupled receptors, a large N-terminal extracellular ectodomain is responsible for hormone recognition. Hormone-receptor pairs have evolved in such a manner that a limited number of positions both at the 'seat-belt' domain of the hormone and the leucine-rich repeats of the receptor, play attractive and repulsive interactions for binding and specificity, respectively. Surprisingly, the constitutive activity of the receptor, mostly modulated by highly conserved amino acids within the heptahelical domain of the receptor (i.e., outside the hormone binding region), also regulates effectiveness of hormone recognition by the extracellular part. In this review we analyze, at the molecular level, these important discriminating determinants for selective binding of glycoprotein hormones to their receptors, as well as natural mutations, observed in patients with gestational hyperthyroidism or ovarian hyperstimulation syndrome, that modify the selectivity of binding. © 2008 Birkhaueser.
Original languageEnglish
Pages (from-to)2484-2492
JournalCellular and Molecular Life Sciences
Volume65
Issue number16
DOIs
Publication statusPublished - 1 Jan 2008

Keywords

  • Gestational hyperthyroidism
  • Glycoprotein hormone receptors
  • Hormone specificity
  • Ovarian hyperstimulation syndrome

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