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- W3037726610 abstract "β-Arrestins (βarrs) critically regulate G-protein-coupled receptor (GPCR) signaling and trafficking. βarrs have two isoforms, βarr1 and βarr2. Receptor phosphorylation is a key determinant for the binding of βarrs, and understanding the intricate details of receptor-βarr interaction is the next frontier in GPCR structural biology. The high-resolution structure of active βarr1 in complex with a phosphopeptide derived from GPCR has been revealed, but that of βarr2 remains elusive. Here, we present a 2.3-Å crystal structure of βarr2 in complex with a phosphopeptide (C7pp) derived from the carboxyl terminus of CXCR7. The structural analysis of C7pp-bound βarr2 reveals key differences from the previously determined active conformation of βarr1. One of the key differences is that C7pp-bound βarr2 shows a relatively small inter-domain rotation. Antibody-fragment-based conformational sensor and hydrogen/deuterium exchange experiments further corroborated the structural features of βarr2 and suggested that βarr2 adopts a range of inter-domain rotations." @default.
- W3037726610 created "2020-07-02" @default.
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- W3037726610 date "2020-09-01" @default.
- W3037726610 modified "2023-10-08" @default.
- W3037726610 title "Crystal Structure of β-Arrestin 2 in Complex with CXCR7 Phosphopeptide" @default.
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- W3037726610 doi "https://doi.org/10.1016/j.str.2020.06.002" @default.
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