Fig. 1

a. Human and Mouse Resistin. Amino acid sequence and secondary structures of human and mouse resistin show differences in folding patterns between the two species. In contrast to the predominantly β-sheet structure of mouse resistin, allowing it to fold in the lollipop-like structure, human resistin contains a majority of α-helices, making it unlikely that the tertiary structures of mouse and human resistin are similar. b: Structural Conformation of Human Resistin and RELMβ. Comparison of the domain structures of Resistin and RELMβ shows 24 % identity in the variable region (purple; V) and 62 % identity in the C-terminal (blue; C) domain. The signal peptide region is indicated in grey (S). The conserved cysteine residues of the C-terminal domain are indicated in yellow. Also indicated in green are the cysteine residues unique to resistin and RELMβ, found in the variable region