Fig. 7: Cartoon diagrams showing a model of the 100K aided hexon folding and assembly. | Nature Communications

Fig. 7: Cartoon diagrams showing a model of the 100K aided hexon folding and assembly.

From: Molecular mechanisms of the viral encoded chaperone 100K in capsid folding and assembly of adenovirus

Fig. 7

100K pre-exists as dimers before engaging with hexon in the cytoplasm. 100K dimers immediately interact with the nascent hexon polypeptides during ribosome synthesis. The 100K dimer forms a complex with the partially folded hexon monomer. This primary 100K-hexon complex serves as a platform for further recruiting additional 100K-bound hexon subunits, ultimately assembling into the immature hexon with 100K. The pre-mature hexon undergoes further conformational changes to release the bound 100K, resulting in the formation of the stable mature hexon. The annotations of the components involved in the cartoon are showed in the bottom.

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