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Egyptian Journal of Medical Human Genetics
Fig. 5 | Egyptian Journal of Medical Human Genetics

Fig. 5

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

Fig. 5

Polar interactions of 3D structures of leptin before mutation and after its being mutated with D76V, C117S, and L161R, in a), b), and c), respectively. Noticeable alterations in the binding capacity between leptin wild-type residue and both D76V and L161R mutants’ residues are found. The C117S mutant residue showed the same binding capacity compared with the wild type residue and the only alteration is found in the distances of this binding. Figures are generated by the measurement tool of PyMol software

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