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. 2022 Sep 12;29(9):942–953. doi: 10.1038/s41594-022-00832-5

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© The Author(s) 2022

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Fig. 2 — a, Bipartite subdomain organization of the Drg1 N domain. b, Electrostatic surface displaying a positively charged (blue) groove of the N-domain model. The binding cleft capturing Arx1 reaches from top to bottom, and ES27 interacts with a positively charged groove spanning both subdomains. c, The N domain of one Drg1 protomer binds Arx1 and ES27 simultaneously. Arx1 loop region 561 to 568 binds into the cleft between Drg1 N_N and N_C. Additional contacts to Drg1 are formed by Arx1 loops 203–219 and 510–521 (light green). The bases U2010 to G2012 of ES27 form a single-stranded loop contacting lysine residues in the Drg1 N domain. d, 3DVA of the Drg1–pre-60S complex. Terminal frames of the 3DVA filtered to 7-Å resolution are superposed.