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Fig. 2 | BMC Ophthalmology

Fig. 2

From: Variants identified by next-generation sequencing cause endoplasmic reticulum stress in Rhodopsin-associated retinitis pigmentosa

Fig. 2

Schematic structural of rhodopsin and predicted crystal structural models of the wild-type and mutants. A Conservation analysis of residues Pro53 and Leu95 across ten species. B Rhodopsin is a light-detecting G-protein-coupled receptor, consisting of a typical seven-transmembrane domain, an extracellular N-terminal tail and a cytoplasmic C-terminal tail. C-D Predicted crystal structural models of the wild-type and mutant p.P53R. E–F Predicted crystal structural models of the wild-type and mutant p.L95P. In comparison with WT, the structure of the L95P mutant protein showed that the hydrogen-bonds between Val87 and Phe91, Phe91 and Leu95, Thr92 and Tyr96 were destroyed (arrowed). G-H The α-helical structure where Leu95 located (boxed) is prematurely interrupted due to mutation to proline according to the structure prediction result

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