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  • Title: Site-directed fluorescence probing to dissect the calcium-dependent association between soluble tissue factor and factor VIIa domains.
    Author: Carlsson K, Osterlund M, Persson E, Freskgård PO, Carlsson U, Svensson M.
    Journal: Biochim Biophys Acta; 2003 May 30; 1648(1-2):12-6. PubMed ID: 12758142.
    Abstract:
    We have used the site-directed labeling approach to study the Ca(2+)-dependent docking of factor VIIa (FVIIa) to soluble tissue factor (sTF). Nine Ca(2+) binding sites are located in FVIIa and even though their contribution to the overall binding between TF and FVIIa has been thoroughly studied, their importance for local protein-protein interactions within the complex has not been determined. Specifically we have monitored the association of the gamma-carboxyglutamic acid (Gla), the first EGF-like (EGF1), and the protease domains (PD) of FVIIa to sTF. Our results revealed that complex formation between sTF and FVIIa during Ca(2+) titration is initiated upon Ca(2+) binding to EGF1, the domain containing the site of highest Ca(2+) affinity. Besides we showed that a Ca(2+)-loaded Gla domain is required for an optimal association of all domains of FVIIa to sTF. Ca(2+) binding to the PD seems to be of some importance for the docking of this domain to sTF.
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