An analysis of the periodicity of conserved residues in sequence alignments of G-protein coupled receptors. Implications for the three-dimensional structure.
Twenty-three sequences from the family of G-protein coupled receptors have been aligned according to the 'historical alignment' procedure of Feng and Doolittle. Fourier transform analysis of this reveals that parts of five of the seven putative membrane-spanning regions exhibit a periodicity of conserved/nonconserved residues which is compatible with the periodicity of the alpha-helix. This would place the conserved residues on one side of the helix, which may face the inside of the proposed seven membered helical bundle.
Donnelly
D
D
Department of Crystallography, Birkbeck College, London, England.
Johnson
M S
MS
Blundell
T L
TL
Saunders
J
J
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D006224:Cricetinae; D005583:Fourier Analysis; D019204:GTP-Binding Proteins; D006801:Humans; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D011943:Receptors, Adrenergic, beta; D011956:Receptors, Cell Surface; D011976:Receptors, Muscarinic; D013552:Swine
D008565:Membrane Proteins; D011943:Receptors, Adrenergic, beta; D011956:Receptors, Cell Surface; D011976:Receptors, Muscarinic; D019204:GTP-Binding Proteins