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. 2007 Apr 2;27(11):4028–4036. doi: 10.1128/MCB.01959-06

FIG. 1.

FIG. 1.

Sequence alignment of horse, human, and pig LEI proteins. By convention, amino acid numbering refers to the PDB nomenclature of serpins that aligns all of the serpins with α1-antitrypsin. UniProtKB/Swiss-Prot entries: horse, LEI P05619; human, LEI P30740; pig, LEI P80229. The hinge region is light green, the inhibitory consensus pattern is dark green, and the P1-P1′ elastase cleavage site is blue. The RCL integrated into the main β-sheet of LEI after cleavage is in bold, and the single elastase recognition site is underlined. His 287, which is lost in human LEI and replaced with Ser, is cyan. The two cysteines of pig LEI are purple. The sequences obtained by Edman degradation are yellow (41). The bipartite NLS is red, and the endonuclease active site is orange. Red arrowheads indicate points of site-directed mutagenesis (1, main NLS mutant; 2, hinge region mutant; 3, endonuclease active-site mutant).