Journal
NATURE COMMUNICATIONS
Volume 5, Issue -, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/ncomms5801
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Funding
- Deutsche Forschungsgemeinschaft [SFB740, SO1037/1-1,2, WO1908/2-1, Hi 1502/1-1, SFB1078-B6]
- European Research Council [ERC-2009/249910-TUDOR]
- European Synchrotron Radiation Facility (ESRF)
- DFG Cluster of Excellence `Unifying Concepts in Catalysis' [D3/E3-1]
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G-protein-coupled receptors (GPCRs) transmit extracellular signals to activate intracellular heterotrimeric G proteins (G alpha beta gamma) and arrestins. For G protein signalling, the G alpha C-terminus (G alpha CT) binds to a cytoplasmic crevice of the receptor that opens upon activation. A consensus motif is shared among GaCT from the G(i)/G(t) family and the 'finger loop' region (ArrFL1-4) of all four arrestins. Here we present a 2.75 angstrom crystal structure ofrrFL-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 GaCT 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.
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