20 Kringle Domain Function In This Year

Kringle domains are triple disulfide linked domains that function as recognition modules for binding other proteins.

Kringle domain function. The name kringle comes from the scandinavian pastry that these structures resemble. Proteins containing kringle domains such as krm1 have various functions and include proteases growth factors and transmembrane receptors nakamura et al 2001. Kringle domains are autonomous protein domains that fold into large loops stabilized by 3 disulfide linkages.

Kringle domains 4 5 6 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. The kringle domain therefore is critical in determining the metabolic fate of under γ carboxylated prothrombin precursors during processing. Solution structure dynamics and function investigation of kringle domain of human receptor tyrosine kinase like orphan receptor 1.

Kringle domains consist of approximately 80 amino acid residues with three disulfide bonds. These are important in protein protein interactions with blood coagulation factors. Enhanced expression of wt gpnmb induced sphere and tumor formation in breast epithelial cells.

Ma x 1 2 liu b 1 2 yang j 3 hu k 1 4. 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. Genic function has yet to be fully elucidated.

1 a state key laboratory of phytochemistry and plant resources in west china kunming institute of botany chinese academy of science kunming. 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. 1 2 3 kringle domains 4 5 6 are characterised by a triple loop 3 disulfide bridge structure whose conformation is defined by a number of hydrogen bonds and small pieces.

In this study we focused on the region the so called kringle like domain kld that is conserved among species and made a deletion mutant gpnmb δkld. The kringle fold occurs in combination with other folds in multidomain proteins often as a part of tandem domains the most frequent number of homologous repeats is 2 and the maximum number of consecutive kringle domains is 37 in apolipoprotein a the kringle family has a broad repertoire of domain partners. The recombinant kringle 5 rk5 domain promotes migration and induces apoptosis of proliferating human microvascular endothelial cells hmevc stimulated with bfgf afgf vegf pdgf tgf β1 il 8 or hgf in a dose dependent manner davidson et al 2005.