Proteins, proteomics

kringle domains

Kringle domains, named for Scandinavian pastries, are conserved sequences that fold into large loops (stabilized by 3 disulfide linkages) the conformation of which is defined by hydrogen bonds and small pieces of anti-parallel β-sheet. Plasminogen-like kringles display affinity for free lysine and for lysine-containing peptides.

Kringle domains are found in several serine proteases, including prothrombin (with two kringle domains) and urokinase-type plasminogen activator, in ROR-like receptors, and they participate in protein-protein interactions with blood coagulation factors.

Urokinase-type plasminogen activator is a strong plasminogen activator which specifically cleaves the proenzyme/zymogen plasminogen to form the active enzyme plasmin.[s] Ror-family RTKs are characterized by the intracellular tyrosine kinase domains, highly related to those of the Trk-family RTKs, and by the extracellular Frizzled-like cysteine-rich domains (CRDs) and Kringle domains.[pm]

[] plasminogen, rotate human plasminogen, primary structure []


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. . . since 11/21/06