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. Author manuscript; available in PMC: 2019 May 21.
Published in final edited form as: Nature. 2018 Nov 21;563(7733):652–656. doi: 10.1038/s41586-018-0743-5

Extended Data Figure 1. Conservation and conformation of D3 C-terminal 𝛂-helix.

Extended Data Figure 1.

(a) Sequence alignment of the C-terminal regions of 14 MAX2/D3 orthologs. Highly conserved residues are colored in blue. (b) Electrostatic potential surface map of D3 with CTH shown in cartoon representation (orange). The C-terminus aspartic acid residue, Asp720, is anchored to a positively charged pocket. (c) Close-up view of the D3 extreme C-terminal residue, Asp720, and its interacting residues in D3 and ASK1. (d) Electron densities of the D3-CTH region in two different crystal forms, adopting either a regular helical conformation (left) or an extended conformation (right).