Title : Characterization of factor VII association with tissue factor in solution. High and low affinity calcium binding sites in factor VII contribute to functionally distinct interactions.

Pub. Date : 1991 Aug 25

PMID : 1874730






6 Functional Relationships(s)
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1 Protein-phospholipid as well as protein-protein interactions may be critical for tight binding of the serine protease factor VIIa (VIIa) to its receptor cofactor tissue factor (TF). Phospholipids coagulation factor III, tissue factor Homo sapiens
2 Protein-phospholipid as well as protein-protein interactions may be critical for tight binding of the serine protease factor VIIa (VIIa) to its receptor cofactor tissue factor (TF). Phospholipids coagulation factor III, tissue factor Homo sapiens
3 Binding of VII occurred with similar affinity to solubilized and phospholipid-reconstituted TF. Phospholipids coagulation factor III, tissue factor Homo sapiens
4 These results suggest that the VII Gla-domain can participate in protein-protein interaction with the TF molecule per se rather than only in interactions with the charged phospholipid surface. 1-Carboxyglutamic Acid coagulation factor III, tissue factor Homo sapiens
5 Interference with Gla-domain-dependent interactions with TF did not alter the TF. 1-Carboxyglutamic Acid coagulation factor III, tissue factor Homo sapiens
6 VIIa-dependent cleavage of a small peptidyl substrate, whereas the proteolytic activation of the protein substrate factor X was markedly decreased, suggesting that the VIIa Gla-domain not only participates in the formation of a more stable TF. 1-Carboxyglutamic Acid coagulation factor III, tissue factor Homo sapiens