Fig. 1
From: Molecular Characterization of a Dual Endothelin-1/Angiotensin II Receptor
Sequences and structural features of the ET-1/AngII receptor. (A) The deduced amino acid sequence is presented underneath the nucleotide sequence with the single hydrophobic (H-l) putative transmembrane domain underlined. The serine and threonine residues with consensus sequences for cAMP-dependent protein kinase (18,19) located within the intracellular domain are highlighted. The regions depicting 12/19 homology with the AngII cRNA-based oligonucleotide probe [1] and 15/23 homology with the ET-1 cRNA-based oligonucleotide probe [2] are marked; identical nucleotides are dotted. Putative AngII and ET-1 binding domains, and internalization recognition sequences (IRS) are bracketed. Amino acids identical to antisense peptide and conservative amino acid substitutions are highlighted (boldface) within corresponding putative binding domains. *, denotes stop codon. (B) Schematic structure of the ET-1/AngII receptor depicting the extracellular, transmembrane, and cytoplasmic domains. The following functional domains are highlighted: putative AngII binding domain, AngII, amino acids 41–48 (red); putative ET-1 binding site, ET-1, amino acids 60–67 (yellow); potential cAMP-dependent protein kinase phosphorylation sites (S91, T108) (green), a potential IRS, [Y111RRP114] (orange), showing homology to the human lysosomal acid phosphatase IRS (21); and amino acids R64 and W65 involved in the site directed mutagenesis. (C) Comparison of the ET-1 and AngII cRNA sequences with the nucleotide and amino acid sequence of the ET-1/AngII receptor identifies aa60–67 and aa41–47 as potential ET-1 and AngII binding domains, respectively. The stippled areas indicate regions of homology. Nucleotides encompassing the ET-1 /AngII receptor ET-1 and AngII binding domains that are present in identical codon position within the corresponding antisense peptide (AP) frames are indicated by asterisks.