Phocid Seal Leptin: Tertiary Structure and Hydrophobic Receptor Binding Site Preservation during Distinct Leptin Gene Evolution
Figure 1
Leptin LEPR-binding residues are conserved across diverse mammalian phyla including the marine mammals.
Summary representative alignment of the predicted amino acid sequences of selected mammalian leptin molecules. Identical residues to human leptin are marked with a dot, spaces manually introduced into the alignment are indicated by ‘-’. Shading represents the leptin residues critical for LEPR binding [24], [25], underlined residues show evidence of positive selection within representatives of the Family Phocidae. The cysteine residues critical for folding are indicated by ▴. The residues that form the helices in the human leptin are marked with a track above the alignment, with the most conserved regions filled. Species for which leptin sequences are reported in this study are underlined. Residue numbering is based on the mature protein from human, residues with a negative placement occur within the signal sequence of the nascent peptide.