An analysis of the periodicity of conserved residues in sequence alignments of G‐protein coupled receptors

FEBS Letters

Johnson, M.S.¹  Saunders, J.²  Blundell, T.L.¹  Donnelly, D.¹ 

[1] Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Steet, London WC1E 7HX, England;Merck Sharp and Dohme Neuroscience Research Centre, Terling Park, Eastwick Road, Harlow CM20 2QR, England

关键词: Primary structure;    Sequence alignment;    Membrane topology;    Membrane-spanning domain;   

DOI  :  10.1016/0014-5793(89)81438-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 α-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.

【 授权许可】

Unknown