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Encyclopedia > Kringle domain

Kringle Domains are conserved sequences that fold into large loops stabilized by 3 disulfide linkages. These are of some importance in protein-protein interactions with blood coagulation factors. The name Kringle comes from the Scandinavian pastry that these structures resemble.


  Results from FactBites:
 
Direct interaction of the kringle domain of urokinase-type plasminogen activator (uPA) and integrin alpha v beta 3 ... (464 words)
The isolated uPA kringle domain binds specifically to purified, recombinant soluble, and cell surface alpha v beta 3, and other integrins (alpha 4 beta 1 and alpha 9 beta 1), and induced migration of CHO cells in an alpha v beta 3-dependent manner.
The binding of the uPA kringle to alpha v beta 3 and uPA kringle-induced alpha v beta 3-dependent cell migration were blocked by homologous plasminogen kringles 1-3 or 1-4 (angiostatin), a known integrin antagonist.
Endothelial cells bound to and migrated on uPA and uPA kringle in an alpha v beta 3-dependent manner.
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