The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A
By M. Weisser, Felix Voigts-Hoffmann, J. Rabl, M. Leibundgut, N. Ban. 2013
88 citations recorded by the source corpus.
Subfields: Molecular Biology
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In Molecular Biology
Citations in the corpus
- Protein Synthesis Initiation in Eukaryotic Cells. (2018, background): “Their cooperative binding induces conformational changes that rotate the head and open up a cleft between the head and body of the 40S to facilitate TC binding (Maag et al. 2005; Passmore et al. 2007; Weisser et al. 2013; Sokabe and Fraser 2014).”
- Toward a Kinetic Understanding of Eukaryotic Translation. (2018, background): “However, other initiation components may contribute to stabilizing this conformation because structures of 40S subunit complexes that include eIF1 and eIF1A adopt a closed conformation (Hashem et al. 2013; Lomakin and Steitz 2013; Weisser et al. 2013).”
- Structural Insights into the Mechanism of Scanning and Start Codon Recognition in Eukaryotic Translation Initiation. (2017, background): “The eIF1A NTT Stabilizes the Codon–Anticodon Helix The globular domain of eIF1A binds to the 40S A site, as demonstrated by DHRC mapping in mammalian PICs [41] and crystal structures of 40S–eIF1–eIF1A complexes from Tetrahymena [42] and mammals [35].”
- Structural Changes Enable Start Codon Recognition by the Eukaryotic Translation Initiation Complex (2014, methodology): “thermophila (Weisser et al., 2013) (Figure S4C) allowed us to build and refine the structure and use it in subsequent analysis.”
- The scanning mechanism of eukaryotic translation initiation. (2014, methodology): “The NMR structures of human eukaryotic initiation factor 1A (eIF1A) (PDB 1D7Q) ( purple) and Tetrahymena eIF1 (PDB 2XZM) (red ) were docked on the 40S subunit in the analogous positions observed in the 30S/eIF1 complex (PDB 1HR0) and the 40S/eIF1 complex (PDB 2XZM), respectively. aIF2β (orange) was ”