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Blood, Vol. 111, Issue 4, 2049-2052, February 15, 2008
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X-ray crystal structure of the fibrinolysis inhibitor {alpha}2-antiplasmin
Blood Law et al. 111: 2049

Supplemental materials for: Law et al.

Files in this Data Supplement:

  • Figure S1. Sequence alignment of α2-antiplasmins and PEDF (PDF. 663 KB) -
    The secondary structures are shown above the alignment, and numbering is for murine 2-antiplasmin. Signal sequences are shaded (grey). N and C-terminal extensions of the serpin domain are boxed (blue). Residues are coloured according to type: polar, green; hydrophobic, yellow; positively charged, blue; and negatively charged, pink. Other indications: black arrow, signal peptide cleavage site; red arrow, secondary cleavage site in plasma 2-antiplasmin; asterisk, the first residue of the protein construct used in the current study; underline, residues missing from the electron density map. Figure is produced with Alscript1.

    Reference
    1. Barton GJ. ALSCRIPT: a tool to format multiple sequence alignments. Protein engineering. 1993;6:37-40.




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