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Fig. 2. Models of serpin structure. (A) Position of nec mutations mapped onto the scaffold of monomeric {alpha}1-antitrypsin (Elliott et al., 2000). The Glu->Lys substitution found in Z-{alpha}1-antitrypsin, nec9 and nec20, maps at the hinge region between the reactive center loop (red) and ß-sheet A (green). ß-sheet B is colored yellow and {alpha}-helix A is blue. NecS>F carries the Ser131->Phe substitution homologous to that of {alpha}1-antitrypsin-Siiyama, Ser53->Phe. (B) Loop-sheet polymer of Z-{alpha}1-antitrypsin and Nec9.





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