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Structure of a β1-adrenergic G-protein-coupled receptor

Nature (London), 2008-07, Vol.454 (7203), p.486-491 [Peer Reviewed Journal]

2008 INIST-CNRS ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/nature07101 ;PMID: 18594507 ;CODEN: NATUAS

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  • Title:
    Structure of a β1-adrenergic G-protein-coupled receptor
  • Author: WARNE, Tony ; SERRANO-VEGA, Maria J ; BAKER, Jillian G ; MOUKHAMETZIANOV, Rouslan ; EDWARDS, Patricia C ; HENDERSON, Richard ; LESLIE, Andrew G. W ; TATE, Christopher G ; SCHERTLER, Gebhard F. X
  • Subjects: Biological and medical sciences ; Crystalline structure ; Fundamental and applied biological sciences. Psychology ; Molecular biophysics ; Structure in molecular biology
  • Is Part Of: Nature (London), 2008-07, Vol.454 (7203), p.486-491
  • Description: G protein-coupled receptors play a major role in transmembrane signalling in higher organisms and many are important drug targets. We report the 2.7 Å resolution crystal structure of a β 1 -adrenergic receptor in complex with the high-affinity antagonist cyanopindolol. The modified turkey receptor had been selected to be in its antagonist conformation and its thermostability improved by earlier limited mutagenesis. The ligand-binding pocket comprises 15 side chains from amino acid residues in 4 transmembrane α-helices and extracellular loop 2. This loop defines the entrance of the ligand-binding pocket and is stabilised by two disulphide bonds and a sodium ion. Cyanopindolol binding to the β 1 -adrenergic receptor and carazolol binding to the β 2 -adrenergic receptor involve similar interactions. A short well-defined helix in cytoplasmic loop 2, not observed in either rhodopsin or the β 2 -adrenergic receptor, directly interacts via a tyrosine with the highly conserved DRY motif at the end of helix 3 that is essential for receptor activation.
  • Publisher: London: Nature Publishing
  • Language: English
  • Identifier: ISSN: 0028-0836
    EISSN: 1476-4687
    DOI: 10.1038/nature07101
    PMID: 18594507
    CODEN: NATUAS
  • Source: ProQuest One Psychology
    Alma/SFX Local Collection
    ProQuest Central
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