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Fig. 4 | Lipids in Health and Disease

Fig. 4

From: Characterization of two ETFDH mutations in a novel case of riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency

Fig. 4

Structure characterization of ETFDH native and mutant proteins. a Sequence alignment among 11 vertebrates (H. sapiens, P. troglodytes, M. mulatta, M. musculus, R. norvegicus, S. scrofa, B. taurus, G. gallus, P. bivittatus, X. Tropicalis, D. rerio) around the site of A187V mutation. The A187 is located in a high conserved region; b Secondary structure of ETFDH(A187V) compared to ETFDH. Missense mutation determines a modification of structure from coiled coil (normal) to α-helix in RR-MADD patient at position 131–134 (indicated by rectangle). The A187V substitution is marked by arrow; c Predicted 3D model of ETFDH, ETFDH (A187V) and ETFDH (G429Dfs21*). The A187V (shown in central tridimensional model) generates conformational alterations of protein folding. The G429Dfs21* lacks the third segment of UQ-binding domain, second membrane-binding surface domain, second part of 4Fe4S cluster and C terminal domain, resulting in a misfolded protein

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