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

Joachim Granzin (), Ursula Wilden, Hui-Woog Choe, Jörg Labahn, Bianca Krafft and Georg Büldt
Additional contact information
Joachim Granzin: Forschungszentrum Jülich, Institut für Biologische Informationsverarbeitung
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

Nature, 1998, vol. 391, issue 6670, 918-921

Abstract: 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.

Date: 1998
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/36147 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:391:y:1998:i:6670:d:10.1038_36147

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/36147

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().