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PDBsum entry 4pxf
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Signaling protein
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PDB id
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4pxf
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References listed in PDB file
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Key reference
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Title
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Crystal structure of a common gpcr-Binding interface for g protein and arrestin.
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Authors
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M.Szczepek,
F.Beyrière,
K.P.Hofmann,
M.Elgeti,
R.Kazmin,
A.Rose,
F.J.Bartl,
D.Von stetten,
M.Heck,
M.E.Sommer,
P.W.Hildebrand,
P.Scheerer.
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Ref.
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Nat Commun, 2014,
5,
4801.
[DOI no: ]
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PubMed id
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Abstract
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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.
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