Fig. 1.
Fig. 1. Factor XIII A-subunit structure and location of common coding polymorphisms. / The structure shown is that of recombinant factor A-subunit dimer, modeled with the use of x-ray crystallography coordinates from Weiss et al.11 The catalytic core region is colored orange; the beta-sandwich, yellow; the 2 beta-barrels, green; and the activation peptide, cyan. Highlighted are the active-site cysteine residue and 5 residues (Val34, Tyr204, Pro564, Val650, and Glu651) that show common variation in the general population (Table2).

Factor XIII A-subunit structure and location of common coding polymorphisms.

The structure shown is that of recombinant factor A-subunit dimer, modeled with the use of x-ray crystallography coordinates from Weiss et al.11 The catalytic core region is colored orange; the beta-sandwich, yellow; the 2 beta-barrels, green; and the activation peptide, cyan. Highlighted are the active-site cysteine residue and 5 residues (Val34, Tyr204, Pro564, Val650, and Glu651) that show common variation in the general population (Table2).

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