Kringle domain

Kringle domains are autonomous <a href="/facts/Protein_domain/oUpFcSsl">protein domains</a> that fold into large <a href="/facts/Loop_(biochemistry)/GdVBHbo3">loops</a> stabilized by 3 disulfide linkages. These are important in <a href="/facts/Protein/Jxmagu3E">protein</a>–protein interactions with blood <a href="/facts/Coagulation/vnfEevM0">coagulation</a> factors. Their name refers to the <a href="/facts/Kringle/avHuUPkm">Kringle</a>, a Scandinavian pastry which they somewhat resemble.
Kringle domains have been found in <a href="/facts/Plasminogen/bfLCyyPt">plasminogen</a>, <a href="/facts/Hepatocyte/USpvDz1n">hepatocyte</a> <a href="/facts/Growth_factor/D1xnRbcH">growth factors</a>, <a href="/facts/Prothrombin/sU9x3MeH">prothrombin</a>, and <a href="/facts/Lipoprotein(a)/fFJ84589">apolipoprotein(a)</a>.
Kringles are found throughout the <a href="/facts/Blood_clotting/vnfEevM0">blood clotting</a> 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. Kringle domains 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.

Kringle domain open-in-new

Kringle domain