Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Fourier Analysis
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GTP-Binding Proteins / metabolism*
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Humans
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Membrane Proteins / chemistry*
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Membrane Proteins / genetics
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Mice
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Molecular Sequence Data
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Multigene Family
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Protein Structure, Secondary*
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Protein Structure, Tertiary
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Rats
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Receptors, G-Protein-Coupled
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Receptors, Gastrointestinal Hormone / chemistry*
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Receptors, Gastrointestinal Hormone / genetics
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Secretin / metabolism*
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Sequence Alignment
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Sequence Homology, Amino Acid
Substances
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Membrane Proteins
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Receptors, G-Protein-Coupled
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Receptors, Gastrointestinal Hormone
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secretin receptor
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Secretin
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GTP-Binding Proteins