Kringle domain
| OPM superfamily | 115 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| OPM protein | 1h8p | ||||||||
| CDD | cd00108 | ||||||||
| |||||||||
Kringle domains are autonomous
loops stabilized by 3 disulfide linkages. These are important in protein–protein interactions with blood coagulation factors. Their name refers to the Kringle
, a Scandinavian pastry which they somewhat resemble.
Kringle domains have been found in
prothrombin, and apolipoprotein(a)
.
Kringles are found throughout the
blood clotting and fibrinolytic proteins. Kringle domains are believed to play a role in binding mediators (e.g., membranes, other proteins or phospholipids), and in the regulation of proteolytic activity.[1][2][3] Kringle domains[4][5][6]
are characterised by a triple loop, 3-disulfide bridge structure, whose conformation is defined by a number of hydrogen bonds and small pieces of anti-parallel beta-sheet. They are found in a varying number of copies in some plasma proteins including prothrombin and urokinase-type plasminogen
activator, which are serine proteases belonging to MEROPS peptidase family S1A.
Human proteins containing this domain
ATF; F12; F2; HABP2; HGF; HGFAC; KREMEN1; KREMEN2;
;