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Fig. 1 | BMC Medical Genetics

Fig. 1

From: Biochemical effects of mutations in the gene encoding the alpha subunit of eukaryotic initiation factor (eIF) 2B associated with Vanishing White Matter disease

Fig. 1

Location of mutations of eIF2Bα on its structure. a Structure of the eIF2Bα dimer showing the location of the mutated residues. All the VWM associated mutations affect sites in the α-helix and β-sheet rich Rossmann-like fold rather than the α-helical bundle furthest from the interaction interface of the homodimer. b The effect of the Asn208Tyr mutation on the proposed phospho-eIF2 binding pocket. The ribbon and spacefill structures show the location of the pocket on the structure of a single monomer of the subunit. The right hand panels show the WT (Asn208) residue relative to the sulphate ion mimicking a phosphate group and a co-ordinating water molecule (upper panel), and the predicted change to the pocket following in silico mutation of Asn208 to Tyr

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