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Structural evidence for visual arrestin priming via complexation of phosphoinositols

Structure. 2021-10; 
Christopher L Sander, Jennings Luu, Kyumhyuk Kim, David Furkert, Kiyoung Jang, Joerg Reichenwallner, MinSoung Kang, Ho-Jun Lee, Bryan T Eger, Hui-Woog Choe, Dorothea Fiedler, Oliver P Ernst, Yong Ju Kim, Krzysztof Palczewski, Philip D Kiser
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Mutant Libraries … coli codon-optimized genes for cysteine-free base mutants (C63V/C128S/C143A, containing two additional mutations, F85A/F197A, which reduce arrestin self-association) were synthesized by GenScript (Piscataway, NJ) and cloned into vector pET-15a between NcoI and XhoI … Get A Quote

摘要

Visual arrestin (Arr1) terminates rhodopsin signaling by blocking its interaction with transducin. To do this, Arr1 translocates from the inner to the outer segment of photoreceptors upon light stimulation. Mounting evidence indicates that inositol phosphates (InsPs) affect Arr1 activity, but the Arr1-InsP molecular interaction remains poorly defined. We report the structure of bovine Arr1 in a ligand-free state featuring a near-complete model of the previously unresolved C-tail, which plays a crucial role in regulating Arr1 activity. InsPs bind to the N-domain basic patch thus displacing the C-tail, suggesting that they prime Arr1 for interaction with rhodopsin and help direct Arr1 translocation. These structu... More

关键词

(1,4,5) myo-D-inositol triphosphate, G protein-coupled receptor, GPCR, InsP(3), InsP(6), arrestin, crystal structure, myo-D-inositol hexakisphosphate, phospholipase C, photoreceptor, phototransduction, retina, vision