Extended Data Fig. 4: nsP1–detergent interactions.
From: Capping pores of alphavirus nsP1 gate membranous viral replication factories
Micelle arrangement and membrane-binding regions of the double-ring structure. a, Lateral section of the double-ring map represented by a green mesh. A section of the map including one detergent micelle is highlighted in blue (left). The central panel shows two symmetry-related nsP1 dimers (n and n + 1) interacting with the FC12 micelle, as a cartoon model coloured in pink and orange. Right, the same as in central panel without the blue mesh, showing the interaction between the two neighbouring nsP1s from each ring and the three cysteines at the tip of the spike. The closest residue between the two rings is C417 from each dimer, with an approximate distance of 4.4 Å between their sulfur atoms. b, Same representation as in a of the entire map, with the view rotated by 90° about the indicated two-fold axis.
