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X-ray crystal structure of arrestin from bovine rod outer segments

Author

Listed:
  • Joachim Granzin

    (Forschungszentrum Jülich, Institut für Biologische Informationsverarbeitung
    Natural Science College, Chonbuk National University)

  • Ursula Wilden

    (Natural Science College, Chonbuk National University)

  • Hui-Woog Choe

    (Forschungszentrum Jülich, Institut für Biologische Informationsverarbeitung)

  • Jörg Labahn

    (Natural Science College, Chonbuk National University)

  • Bianca Krafft

    (Natural Science College, Chonbuk National University)

  • Georg Büldt

    (Natural Science College, Chonbuk National University)

Abstract

Retinal arrestin is the essential protein for the termination of the light response in vertebrate rod outer segments. It plays an important role in quenching the light-induced enzyme cascade by its ability to bind to phosphorylated light-activated rhodopsin (P-Rh*). Arrestins are found in various G-protein-coupled amplification cascades. Here we report on the three-dimensional structure of bovine arrestin (relative molecular mass, 45,300) at 3.3 Å resolution. The crystal structure comprises two domains of antiparallel β-sheets connected through a hinge region and one short α-helix on the back of the amino-terminal fold. The binding region for phosphorylated light-activated rhodopsin is located at the N-terminal domain, as indicated by the docking of the photoreceptor to the three-dimensional structure of arrestin. This agrees with the interpretation of binding studies on partially digested and mutated arrestin.

Suggested Citation

  • Joachim Granzin & Ursula Wilden & Hui-Woog Choe & Jörg Labahn & Bianca Krafft & Georg Büldt, 1998. "X-ray crystal structure of arrestin from bovine rod outer segments," Nature, Nature, vol. 391(6670), pages 918-921, February.
    • Handle: RePEc:nat:nature:v:391:y:1998:i:6670:d:10.1038_36147
    DOI: 10.1038/36147
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