Mutagenesis of the beta2-Adrenergic Receptor: How Structure Elucidates Function

A novel G protein-coupled receptor for gonadotropin-inhibitory hormone in the Japanese quail (Coturnix japonica): identification, expression and binding activity

“…1A and depicted as seven hydrophobic peaks in Fig. 1B), connected by three cytosolic and three extracellular loops, extracellular N-terminal and cytosolic C-terminal domains that are characteristic of GPCRs (Ostrowski et al 1992, Sun et al 2001. The predicted initiator methionine codon agreed with Kozak's first-AUG rule (Kozak 1989).…”

“…The deduced amino acid sequence of the quail GnIH receptor showed a higher homology to the receptors for rat and human RFRP (full length, 68%; TMs, 81-86%) than to those for rat and human NPFF (full length, 48-50%; TMs, 71-73%). The seven transmembrane-spanning domains are suggested to be oriented to form a ligandbinding pocket (Ostrowski et al 1992, Watson & Arkinstall 1994. The C-terminal LPXRF-amide motif of GnIH and RFRP may be a reason for a higher homology of the structure of TMs of these receptors.…”

Molecular cloning and functional characterization of V2 [8‐lysine] vasopressin and oxytocin receptors from a pig kidney cell line

“…This divergence cannot be attributed only to species differences, because oxytocin receptors, that belong to the same subfamily and have been cloned from the same species, have a similar identity for both N-terminal and C-terminal regions, of 86.5% and 81 %, respectively. Studies primarily performed on adrenergic and muscarinic receptors suggest that the N-terminal part of G-protein-coupled receptors for catecholamines and acetylcholine is responsible for the transport of receptors to the cell membrane, but contains no determinants for ligand binding (Ostrowski et al, 1992). However, for receptors that recognize peptide hormones, the importance of the N-terminal region for ligand binding has been shown : for the lutropin-choriogonadotropin receptor (Xie et al, 1990;Nagayama et al, 1991) and recently for tachikinin and endothelin-receptor subfamilies (Yokota et al, 1992;Hashido et al, 1992).…”

Structure, function, and regulation of adrenergic receptors

“…A detailed description of all available information on adrenergic receptors would clearly go beyond the scope of this article and can be found in a number of recent reviews (Harrison et al, 1991;Strosberg, 1991b;Bylund, 1992;Kobilka, 1992;Ostrowski et al, 1992), but I have attempted to summarize in Table 1 some of the salient features of the human adrenergic receptors and will discuss below further molecular characteristics of the ligandbinding and G protein-coupling domains. In this table, 1 present pharmacologic properties in terms of agonists and agonists reported to bind to or stimulate one subtype better than any other subtype with the caveat that no single drug suffices to define a given receptor.…”