Molecular Properties of the CRF Receptor

• Published in: Trends in endocrinology and metabolism Vol. 9; no. 4; pp. 140 - 145
• Main Authors: Spiess, Joachim, Dautzenberg, Frank M, Sydow, Sabine, Hauger, Richard L, Rühmann, Andreas, Blank, Thomas, Radulovic, Jelena
• Format: Journal Article
• Language: English
• Published: London Elsevier Ltd 01.05.1998; Elsevier
• Subjects: Biological and medical sciences; CRF; CRF binding; CRF ligand specificity; CRF receptor; CRF receptor desensitization; CRF receptor evolution; Fundamental and applied biological sciences. Psychology; Hormones and neuropeptides. Regulation; Hypothalamus. Hypophysis. Epiphysis. Urophysis; urocortin; Vertebrates: endocrinology; urocortin; CRF receptor; CRF receptor evolution; CRF binding; CRF; CRF ligand specificity; CRF receptor desensitization; Hypothalamic hormone; Ligand binding; ACTH-RH; Binding site; Review; Hormone releasing factor; Subtype; Polymorphism; Biological receptor
• ISSN: 1043-2760; 1879-3061
• DOI: 10.1016/S1043-2760(98)00037-X

Research into the biology of corticotropin-releasing factor (CRF) has been intensified significantly by the structural characterization of the CRF receptor (CRF-R). Two receptor subtypes, CRF-R1 and CRF-R2, and three functional splice variants of CRF-R2 have been discovered. It appears that ligand binding requires interaction of the N-terminal domain with one or two other extracellular domains of the CRF-R. In contrast to the mammalian CRF-R1, the frog CRF-R1 discriminates between naturally occurring CRF-like peptides.