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Figure 2 | Molecular Medicine

Figure 2

From: Feline Congenital Erythropoietic Porphyria: Two Homozygous UROS Missense Mutations Cause the Enzyme Deficiency and Porphyrin Accumulation

Figure 2

Effect of the individual and combined CEP mutations on the predicted three-dimensional structures of feline URO synthase. Each of the three panels are overlays of the wild-type structure and one of the mutant structures in the region of cluster 2, containing amino acids Lys 88, Ile 110 and Gly 111. (A) Comparison of the wild-type structure (residues colored in gray) with the S47F structure (residues colored in orange). (B) Comparison of the wild-type structure with the G111S structure (residues colored in green). (C) Comparison of the wild-type structure with the S47F/G111S structure (residues colored in blue). Note particularly that the position of Serine 111 in the structure of the combined S47F/G111S mutation structure is intermediate in position between that of the wild-type Glycine 111 and the Serine 111 of the G111S structure.

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