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The c-carboxyglutamic acid domain of human factor VIIa is essential for its interaction with cell surface tissue factor


The c-carboxyglutamic acid domain of human factor VIIa is essential for its interaction with cell surface tissue factor



The Journal of Biological Chemistry 265: 90-4




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Accession: 018161930

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Related references

The gamma-carboxyglutamic acid domain of human factor VIIa is essential for its interaction with cell surface tissue factor. Journal of Biological Chemistry 265(4): 1890-1894, 1990

Influence of the gamma-carboxyglutamic acid-rich domain and hydrophobic stack of factor VIIa on tissue factor binding. Haemostasis 26 Suppl. 1: 31-34, 1996

Conformation of factor VIIa stabilized by a labile disulfide bond (Cys-310-Cys-329) in the protease domain is essential for interaction with tissue factor. Journal of Biological Chemistry 272(41): 25724-25730, 1997

Tissue factor positions and maintains the factor VIIa active site far above the membrane surface even in the absence of the factor VIIa Gla domain. A fluorescence resonance energy transfer study. Journal of Biological Chemistry 272(48): 30160-30166, 1997

Roles of the membrane-interactive regions of factor VIIa and tissue factor. The factor VIIa Gla domain is dispensable for binding to tissue factor but important for activation of factor X. Journal of Biological Chemistry 269(11): 8007-8013, 1994

Substrate recognition by tissue factor-factor VIIa. Evidence for interaction of residues Lys165 and Lys166 of tissue factor with the 4-carboxyglutamate-rich domain of factor X. Journal of Biological Chemistry 271(36): 21752-21757, 1996

Inhibitory properties of full-length and truncated recombinant tissue factor pathway inhibitor (TFPI). Evidence that the third Kunitz-type domain of TFPI is not essential for the inhibition of factor VIIa-tissue factor complexes on cell surfaces. Journal of Biological Chemistry 268(12): 8704-8710, 1993

First epidermal growth factor-like domain of human blood coagulation factor IX is required for its activation by factor VIIa/tissue factor but not by factor XIa. Proceedings of the National Academy of Sciences of the United States of America 91(9): 3574-3578, 1994

Structurally and Functionally Distinct Ca2+ Binding Sites in the -Carboxyglutamic Acid-Containing Domain of Factor VIIa. Febs Journal 234(1): 293-300, 1995

Platelet factor 4 binds to the gamma-carboxyglutamic acid domain of factor X and impairs tissue factor -mediated coagulation Possible role as a physiologic anticoagulant. Blood 84(10 Suppl. 1): 532A, 1994

Spectroscopic probing of the influence of calcium and the Gla domain on the interaction between the first EGF domain in factor VIIa and tissue factor. European Journal of Biochemistry 267(20): 6204-6211, 2000

Structurally and functionally distinct Ca2+ binding sites in the gamma-carboxyglutamic acid-containing domain of factor VIIa. European Journal of Biochemistry 234(1): 293-300, 1995

Substitution of the Gla domain in factor X with that of protein C impairs its interaction with factor VIIa/tissue factor: lack of comparable effect by similar substitution in factor IX. Journal of Biological Chemistry 282(21): 15632-15644, 2007

Factor VIIa-induced p44/42 mitogen-activated protein kinase activation requires the proteolytic activity of factor VIIa and is independent of the tissue factor cytoplasmic domain. Journal of Biological Chemistry 274(30): 21349-21354, 1999

VIIa/tissue factor interaction results in a tissue factor cytoplasmic domain-independent activation of protein synthesis, p70, and p90 S6 kinase phosphorylation. Journal of Biological Chemistry 277(30): 27065-27072, 2002