Kringles [1,2,3] are triple-looped, disulfide cross-linked domains found in a
varying number of copies, in some serine proteases and plasma proteins. The
kringle domain has been found in the following proteins:
Apolipoprotein A (38 copies).
Blood coagulation factor XII (Hageman factor) (1 copy).
Hepatocyte growth factor (HGF) (4 copies).
Hepatocyte growth factor like protein (4 copies) .
'C': conserved cysteine involved in a disulfide bond.
Kringle domains are thought to play a role in binding mediators, such as
membranes, other proteins or phospholipids, and in the regulation of
proteolytic activity. As a signature pattern for this type of domain, we
selected a conserved sequence that contains two of the cysteines invovled in
Friezner Degen S.J., Stuart L.A., Han S., Jamison C.S.
Miyazawa K., Shimomura T., Kitamura A., Kondo J., Morimoto Y., Kitamura N.
Molecular cloning and sequence analysis of the cDNA for a human serine protease reponsible for activation of hepatocyte growth factor. Structural similarity of the protease precursor to blood coagulation factor XII.
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