NDLI: Mapping of the ligand-selective domain of the Xenopus laevis corticotropin-releasing factor receptor 1: implications for the ligand-binding site.

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Mapping of the ligand-selective domain of the Xenopus laevis corticotropin-releasing factor receptor 1: implications for the ligand-binding site.

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Mapping of the ligand-selective domain of the Xenopus laevis corticotropin-releasing factor receptor 1: implications for the ligand-binding site.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dautzenberg, F. M. Spiess, J. Wille, S. Lohmann, R.
Description	Author Affiliation: Dautzenberg FM ( Max-Planck Institute for Experimental Medicine, Department of Molecular Neuroendocrinology, Hermann-Rein-Strasse 3, 37075 Goettingen, Germany. Dautzenberg@mail.mpiem.gwdg.de);
Abstract	The nonselective human corticotropin-releasing factor receptor 1 (hCRF-R1) and the ligand-selective Xenopus CRF-R1 (xCRF-R1) were compared. To understand the interactions of sauvagine and ovine CRF, both high-affinity ligands for hCRF-R1 but surprisingly weak ligands for xCRF-R1, chimeric receptors of hCRF-R1 and xCRF-R1 followed by double or multiple point mutations were constructed. Binding studies and cAMP assays demonstrated that the N-terminal domain exhibited the complete ligand selectivity of xCRF-R1. The important region was mapped between amino acids 70 and 89; replacement of amino acids Arg76, Asn81, Gly83, Leu88, and Ala89 in hCRF-R1 with the corresponding amino acids of xCRF-R1 (Gln76, Gly81, Val83, His88, and Leu89) resulted in a receptor that had approximately 30-fold higher affinity for human/rat CRF than for sauvagine. Mutagenesis of these amino acids in xCRF-R1 to the human sequence completely abolished the ligand selectivity of xCRF-R1. Mutagenesis of amino acids 88 and 89 in hCRF-R1 or xCRF-R1 had only a minor (approximately 2.5-fold) effect on the ligand selectivity of the mutant receptor. Substitution of Arg76, Asn81, and Gly83 in hCRF-R1 with the corresponding sequence of xCRF-R1 (Gln76, Gly81, and Val83) resulted in a receptor with approximately 11-fold higher affinity for human/rat CRF compared with ovine CRF or sauvagine. When only two of these three amino acids were mutated, no effect on the ligand selectivity was observed. On the basis of these data, it is suggested that amino acids 70-89 of CRF-R1 are important for the ligand binding site.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	95
Language	English
Publisher	National Academy of Sciences
Publisher Date	1998-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Receptors, Corticotropin-Releasing Hormone Chemistry Amino Acid Sequence Amphibian Proteins Animals Binding Sites Binding, Competitive Cell Line Corticotropin-Releasing Hormone Metabolism Cyclic AMP Ligands Molecular Sequence Data Peptide Hormones Peptides Recombinant Fusion Proteins Species Specificity Structure-Activity Relationship Xenopus Laevis Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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