Extended Data Fig. 6: eRF1 secondary structure and alignments.
From: The eRF1 degrader SRI-41315 acts as a molecular glue at the ribosomal decoding center
Sequence alignments of eRF1 from the indicated species (H. sapiens UniProt P62495; O. cuniculus UniProt P62497; M. musculus UniProt Q8BWY3; X. laevis UniProt P35615; D. rerio UniProt Q803E5; D. melanogaster UniProt Q9VPH7; C. elegans UniProt O16520; S. cerevisiae UniProt P12385) with secondary structure designations above colored based on their presence in the N (blue), M (green), and C (orange) domains of eRF1. In the accommodated state of eRF1, α8 of the M domain and α9 of the C domain form a continuous helix (yellow). eRF1 also contains a minidomain insertion (gray) in the C domain that is not present in structurally similar decoding factors. In the N domain, Met51 (purple arrowhead) involved in SRI-41315 binding, as well as the NIKS and YxCxxxF motifs (gray lines) and Glu55 (gray arrowhead) involved in stop codon recognition, are indicated below. Note: human, rabbit, and mouse eRF1 are 100% identical. Part of the C-terminal extension in C. elegans eRF1 is not shown.
