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Model of HK1-clustering. Lack of ATP or mutation in the ATP-binding site favors an open conformation of the C-terminal half and is an initial step of HK1-clustering. Further depletion of ATP or mutation in the dimeric interface leads to dimer-monomer-transition. Monomeric HK1 forms new oligomers that assemble into HK1-clusters. HK1-clustering is reversed by ATP or G6P. Data are presented as mean SD.

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