Functional domains of the gonadotropin-releasing hormone receptor

S C Sealfon, Sealfon SC, Robert P. Millar, R P Millar
Cellular and molecular neurobiology · 1995 · vol. 15(1) , pp. 25–42 · doi:10.1007/bf02069557 · PMID:7648608 · PMC11563151
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This paper characterizes the mammalian gonadotropin-releasing hormone receptor as a 327- to 328-amino acid seven-transmembrane G protein-coupled receptor, detailing insights into its glycosylation, helical arrangement, and ligand binding domains.

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Abstract

1. The cloning of the mammalian gonadotropin-releasing hormone receptor sets the stage for rapid progress in understanding the structure of the receptor, its interaction with ligand, and its mechanisms of activation. 2. The receptor is a 327 to 328-amino acid seven-transmembrane domain G protein-coupled receptor. 3. Recent site-direct mutagenesis studies have provided considerable insight into glycosylation of the receptor, the arrangement of the helices, and the ligand binding domains.

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MeSH descriptors

Receptors, LHRH Receptors, LHRH Amino Acid Sequence Animals Cattle Cloning, Molecular Humans Mammals Mice Molecular Sequence Data Protein Conformation Rats Receptors, LHRH Recombinant Proteins Recombinant Proteins Recombinant Proteins Sequence Homology, Amino Acid Sheep

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europepmc
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pubmed
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