Author
Listed:
- Michal Szczepek
(Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1)
- Florent Beyrière
(Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1)
- Klaus Peter Hofmann
(Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1
Zentrum für Biophysik und Bioinformatik, Humboldt-Universität zu Berlin, Invalidenstrasse 42)
- Matthias Elgeti
(Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1
Present address: Department of Chemistry and Biochemistry, Jules Stein Eye Institute, University of California, Los Angeles, California 90095-700, USA)
- Roman Kazmin
(Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1)
- Alexander Rose
(Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1
Institut für Medizinische Physik und Biophysik (CC2), AG ProteiInformatics, Charité-Universitätsmedizin Berlin, Charitéplatz 1)
- Franz J. Bartl
(Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1
Zentrum für Biophysik und Bioinformatik, Humboldt-Universität zu Berlin, Invalidenstrasse 42)
- David von Stetten
(Structural Biology Group, European Synchrotron Radiation Facility, CS 40220)
- Martin Heck
(Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1)
- Martha E. Sommer
(Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1)
- Peter W. Hildebrand
(Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1
Institut für Medizinische Physik und Biophysik (CC2), AG ProteiInformatics, Charité-Universitätsmedizin Berlin, Charitéplatz 1)
- Patrick Scheerer
(Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1
Institut für Medizinische Physik und Biophysik (CC2), AG Protein X-ray Crystallography, Charité-Universitätsmedizin Berlin, Charitéplatz 1)
Abstract
G-protein-coupled receptors (GPCRs) transmit extracellular signals to activate intracellular heterotrimeric G proteins (Gαβγ) and arrestins. For G protein signalling, the Gα C-terminus (GαCT) binds to a cytoplasmic crevice of the receptor that opens upon activation. A consensus motif is shared among GαCT from the Gi/Gt family and the ‘finger loop’ region (ArrFL1–4) of all four arrestins. Here we present a 2.75 Å crystal structure of ArrFL-1, a peptide analogue of the finger loop of rod photoreceptor arrestin, in complex with the prototypical GPCR rhodopsin. Functional binding of ArrFL to the receptor was confirmed by ultraviolet-visible absorption spectroscopy, competitive binding assays and Fourier transform infrared spectroscopy. For both GαCT and ArrFL, binding to the receptor crevice induces a similar reverse turn structure, although significant structural differences are seen at the rim of the binding crevice. Our results reflect both the common receptor-binding interface and the divergent biological functions of G proteins and arrestins.
Suggested Citation
Michal Szczepek & Florent Beyrière & Klaus Peter Hofmann & Matthias Elgeti & Roman Kazmin & Alexander Rose & Franz J. Bartl & David von Stetten & Martin Heck & Martha E. Sommer & Peter W. Hildebrand &, 2014.
"Crystal structure of a common GPCR-binding interface for G protein and arrestin,"
Nature Communications, Nature, vol. 5(1), pages 1-8, December.
Handle:
RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5801
DOI: 10.1038/ncomms5801
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