1997
DOI: 10.1016/s0014-5793(97)00941-1
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Abstract: concentrations. The light chain of fVIIa associated 5-fold slower with sTF than did fVIIa at saturating Ca 2+ concentrations, whereas the dissociation of its complex with sTF was at least 100-fold faster than that of fVIIa:sTF. This gave a dissociation constant of 1-2 uM for the interaction between the light chain and sTF compared to about 3 nM for the fVIIa:sTF interaction.

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Cited by 13 publications
(17 citation statements)
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References 43 publications
(75 reference statements)
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“…These calcium ions participate in the formation of the Glacalcium network. The effect of the calcium ions on the structure and function of factor VIIa and the affinities of the calcium binding have been subjected to extensive studies by several laboratories (Cheung and Stafford, 1995;Persson and Petersen, 1995;Persson, 1996Persson, , 1997Petersen and Persson, 1996;Freskgard et al, 1998;Inoue et al, 1996). Geng and Castellino (1997) studied the lipid-binding properties of a recombinant chimeric protein in which the Gla and helical stack domains of human anticoagulant protein C were replaced by those of human factor VII.…”
Section: Gla Domainmentioning
confidence: 99%
“…These calcium ions participate in the formation of the Glacalcium network. The effect of the calcium ions on the structure and function of factor VIIa and the affinities of the calcium binding have been subjected to extensive studies by several laboratories (Cheung and Stafford, 1995;Persson and Petersen, 1995;Persson, 1996Persson, , 1997Petersen and Persson, 1996;Freskgard et al, 1998;Inoue et al, 1996). Geng and Castellino (1997) studied the lipid-binding properties of a recombinant chimeric protein in which the Gla and helical stack domains of human anticoagulant protein C were replaced by those of human factor VII.…”
Section: Gla Domainmentioning
confidence: 99%
“…The crystal structure of fVIIa in complex with the extracellular part of TF (sTF) reveals an extensive interface between the two proteins encompassing all four domains in fVIIa, with the light chain contributing the majority of the binding energy (5), and both extracellular domains of TF (6,7). The intradomain structural changes that accompany the allosteric enhancement of fVIIa's activity appear to be confined to the protease domain (8), but the precise molecular switch by which TF turns on fVIIa remains elusive.…”
mentioning
confidence: 99%
“…As increasing temperature favours hydrophobic interctions and disfavours hydrophilic interactions [24], this explanation might relate to the FVIIa–TF X‐ray structure which shows that the interaction of TF with the protease domain of FVIIa is mainly polar, whereas the interface with the first EGF‐like and the Gla domain is predominantly of a hydrophobic nature [20]. In this context it is worth noting that binding studies with the isolated light chain of FVIIa suggests that the protease domain accounts for approximately 30% of the total energy gain associated with complex formation [11], and destabilization of the interaction between TF and the protease domain by heating is apparently sufficient to produce a significant decline in overall binding as monitored by the sensitive ELISA (Fig. 4).…”
Section: Discussionmentioning
confidence: 99%
“…The catalytic activity increases profoundly when FVIIa binds to TF as first demonstrated with the chromogenic substrate, d ‐isoleucyl‐ l ‐prolyl‐ l ‐arginine p ‐nitroanilide (Ile‐Pro‐Arg‐NH‐Np) [8]. Ca 2+ ions are also needed for optimal stimulation of FVIIa activity by TF as the formation of a high‐affinity complex requires binding of Ca 2+ to the epidermal growth factor (EGF)‐like [9,10] and γ‐carboxyglutamic acid (Gla) domains [11] of FVIIa. Interestingly, the Ca 2+ dependency of FVIIa amidolytic activity is abrogated when TF is bound and chemically cross‐linked to FVIIa [12].…”
mentioning
confidence: 99%