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- W1990245422 abstract "Cotranslational targeting of membrane and secretory proteins is mediated by the universally conserved signal recognition particle (SRP). Together with its receptor (SR), SRP mediates the guanine triphosphate (GTP)-dependent delivery of translating ribosomes bearing signal sequences to translocons on the target membrane. Here, we present the crystal structure of the SRP:SR complex at 3.9 angstrom resolution and biochemical data revealing that the activated SRP:SR guanine triphosphatase (GTPase) complex binds the distal end of the SRP hairpin RNA where GTP hydrolysis is stimulated. Combined with previous findings, these results suggest that the SRP:SR GTPase complex initially assembles at the tetraloop end of the SRP RNA and then relocalizes to the opposite end of the RNA. This rearrangement provides a mechanism for coupling GTP hydrolysis to the handover of cargo to the translocon." @default.
- W1990245422 created "2016-06-24" @default.
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- W1990245422 date "2011-02-18" @default.
- W1990245422 modified "2023-10-16" @default.
- W1990245422 title "The Crystal Structure of the Signal Recognition Particle in Complex with Its Receptor" @default.
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- W1990245422 doi "https://doi.org/10.1126/science.1196473" @default.
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