| Type: | Conserved_site | Name: | Kringle, conserved site |
| Description: | Kringles are autonomous structural domains, 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 [, , ]. Kringle domains [, , ] are characterised by a triple loop, 3-disulphide 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.This entry represents a conserved site within the kringle domain that contains two of the cysteines involved in disulphide bonds. | Short Name: | Kringle_CS |
| DB identifier | Type | Name |
|---|---|---|
| IPR013806 | Domain | Kringle-like fold |
| IPR001314 | Family | Peptidase S1A, chymotrypsin-type |
| IPR000001 | Domain | Kringle |
| IPR003966 | Family | Prothrombin/thrombin |
| IPR016247 | Family | Tyrosine-protein kinase, receptor ROR |
| IPR014394 | Family | Coagulation factor XIIa/hepatocyte growth factor activator |
| IPR017076 | Family | Kremen |
