The arrestin-receptor complex: Exciting answers and new questions
The Structural Basis of Arrestin Functions, Page: 175-184
2017
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Book Chapter Description
To better understand the molecular mechanism of arrestin-mediated signaling, detailed structural information on the arrestin-receptor complex is necessary. Biochemical studies provided some information about how arrestins are recruited by active receptors. The X-ray laser crystal structure of the rhodopsinarrestin complex reveals unique structural features, which include the asymmetric binding of arrestin to rhodopsin. Arrestin adopts the active conformation, with a ~20° rotation between the N- and C-domains of the molecule, which opens up a cleft in arrestin to accommodate a short helix formed by the second intracellular loop of rhodopsin. Rhodopsin-arrestin complex gives important insights into how G protein-coupled receptor signaling is terminated by arrestin and reveals structural basis of the mechanism of arrestin-biased signaling.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85033994359&origin=inward; http://dx.doi.org/10.1007/978-3-319-57553-7_13; http://link.springer.com/10.1007/978-3-319-57553-7_13; https://dx.doi.org/10.1007/978-3-319-57553-7_13; https://link.springer.com/chapter/10.1007/978-3-319-57553-7_13
Springer Science and Business Media LLC
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