Fig. 4: Four molecules of Nup93 interact with Nup188 and Nup205 to form the central scaffold.
From: Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex
a Overall distribution of four Nup93 molecules in the IR subunit. On the cytoplasmic side, Nup93-1 and Nup93-2 interact with Nup188 and Nup205, respectively. b Structure of Nup93. Shown here is a cartoon representation of Nup93-1. The short N-terminal helix is known to interact with CNT.13 The extended N-terminal helix α5 binds Nup188 or Nup205. c A close-up view on the asymmetric interface between Nup93-1 and Nup93-2. d A close-up view on the interface between Nup93-1 and Nup188. Notably, helix α5 of Nup93-1 is placed in the axial groove of the Nup188 α-solenoid and interacts with the C-terminal helices of Nup188. e A close-up view on the interface between Nup93-2 and Nup205. In striking analogy to the Nup93-1/Nup188 interface, helix α5 of Nup93-2 is placed in the axial groove of the Nup205 α-solenoid and interacts with the C-terminal helices of Nup205. f A side-by-side comparison of the interaction between helix α5 of Nup93 and Nup188 (upper panel) or Nup205 (lower panel). Nup188 and Nup205 are shown in surface representation.
