The arrangement of the transmembrane helices in the secretin receptor family of G-protein-coupled receptors.
The members of the secretin receptor family of G-protein-coupled receptors share no significant sequence similarity to the more familiar rhodopsin-like family. However, multiple sequence alignment analysis reveals seven hydrophobic regions with significant alpha-helical periodicity. Residues that are likely to be buried on the interior of the helical bundle and others that are likely to contact the lipid bilayer are identified. A predicted arrangement of the helical bundle is described in which, by comparison with the arrangement in the rhodopsin family, helices 2 and 7 are more buried within the bundle while helix 3 is more exposed to the lipid bilayer.
Donnelly
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Department of Pharmacology, University of Leeds, UK. d.donnelly@leeds.ac.uk
D000595:Amino Acid Sequence; D000818:Animals; D005583:Fourier Analysis; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics; D051379:Mice; D008969:Molecular Sequence Data; D005810:Multigene Family; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D051381:Rats; D043562:Receptors, G-Protein-Coupled; D011964:Receptors, Gastrointestinal Hormone / Q000737:chemistry* / Q000235:genetics; D012633:Secretin / Q000378:metabolism*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D008565:Membrane Proteins; D043562:Receptors, G-Protein-Coupled; D011964:Receptors, Gastrointestinal Hormone; C029937:secretin receptor; D012633:Secretin; D019204:GTP-Binding Proteins