Conserved Site

Kringle, conserved site (IPR018056)

Short name: Kringle_CS


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 [PMID: 3886654, PMID: 6373375, PMID: 2157850]. Kringle domains [PMID: 3131537, PMID: 3891096, PMID: 1879523] 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.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns