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Fig. 2 | Egyptian Journal of Medical Human Genetics

Fig. 2

From: D76V, L161R, and C117S are the most pathogenic amino acid substitutions with several dangerous consequences on leptin structure, function, and stability

Fig. 2

The positioning of the most deleterious amino acid substitutions identified in leptin. a) Evolutionary conservation pattern of amino acid residues within the primary sequence of leptin. Color intensity increases with degree of conservation. The amino acids are colored based on their conservation grades and conservation levels. The amino acid positions of the most three deleterious predicted SNPs are maximized below the protein sequence. Both C117 and L161 residues showed higher conserved positions compared with D76 residue. b) Secondary structure prediction of leptin. Both D76 and L161 amino acid residues are positioned in the alpha-helix region, while the C117 amino acid residue is suited in the highly critical cysteine-cysteine junction. The primary and secondary structures are generated by ConSurf and PolyView-2D tools, respectively

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