FigureĀ 2.
(A) In the presence of ATP, IMPDH2 assembles extended octamer filaments. Binding of GTP leads to assembly of compressed octamer filaments that remain partially active where the tetramer is in a flat conformation. In the presence of very high GTP concentrations, the tetramer is completely inhibited and enters a bowed conformation which promotes disassembly of the filament into free octamers [5] (B) For canonical IMPDH1, binding of ATP drives assembly of a filament composed of extended octamers. In the presence of GTP, canonical IMPDH1 assembles into a filament with the small interface made of fully compressed octamers that are mostly inhibited and have the bowed tetramer conformation. Figure adapted from [6].
Model of IMPDH1 isoform assembly and filament role in regulation.

(A) In the presence of ATP, IMPDH2 assembles extended octamer filaments. Binding of GTP leads to assembly of compressed octamer filaments that remain partially active where the tetramer is in a flat conformation. In the presence of very high GTP concentrations, the tetramer is completely inhibited and enters a bowed conformation which promotes disassembly of the filament into free octamers [5] (B) For canonical IMPDH1, binding of ATP drives assembly of a filament composed of extended octamers. In the presence of GTP, canonical IMPDH1 assembles into a filament with the small interface made of fully compressed octamers that are mostly inhibited and have the bowed tetramer conformation. Figure adapted from [6].

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