4pxf

Crystal structure of the active G-protein-coupled receptor opsin in complex with the finger-loop peptide derived from the full-length arrestin-1

spinqualitylabelsall models 4pxf, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pxf is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, BMA, BOG, PLM, SO4, TRE, MAN, NAG Resources: FirstGlance, OCA, RCSB, PDBsum Disease [ARRS_BOVIN] Note=S-antigen induces autoimmune uveitis. Function [OPSD_BOVIN] Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity). [ARRS_BOVIN] Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase. Isoform B plays a role in the phototransduction cascade. Publication Abstract from PubMed G-protein-coupled receptors (GPCRs) transmit extracellular signals to activate intracellular heterotrimeric G proteins (Galphabetagamma) and arrestins. For G protein signalling, the Galpha C-terminus (GalphaCT) binds to a cytoplasmic crevice of the receptor that opens upon activation. A consensus motif is shared among GalphaCT from the Gi/Gt family and the 'finger loop' region (ArrFL1-4) of all four arrestins. Here we present a 2.75 A 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 GalphaCT 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. Crystal structure of a common GPCR-binding interface for G protein and arrestin.,Szczepek M, Beyriere F, Hofmann KP, Elgeti M, Kazmin R, Rose A, Bartl FJ, von Stetten D, Heck M, Sommer ME, Hildebrand PW, Scheerer P Nat Commun. 2014 Sep 10;5:4801. doi: 10.1038/ncomms5801. PMID:25205354 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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