ArticleProtein science : a publication of the Protein Society1996
Structural changes in factor VIIa induced by Ca2+ and tissue factor studied using circular dichroism spectroscopy.
Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 55 citations in OpenAlex.
- A bispecific antibody approach for the potential prophylactic treatment of inherited bleeding disorders.Nature cardiovascular research · 2024Article
- A systematic approach for evaluating the role of surface-exposed loops in trypsin-like serine proteases applied to the 170 loop in coagulation factor VIIa.Scientific reports · 2022Article
- Zymogen and activated protein C have similar structural architecture.The Journal of biological chemistry · 2020Article
- Beating tissue factor at its own game: Design and properties of a soluble tissue factor-independent coagulation factor VIIa.The Journal of biological chemistry · 2020Article
- Bioengineering of rFVIIa Biopharmaceutical and Structure Characterization for Biosimilarity Assessment.Bioengineering (Basel, Switzerland) · 2018Article
- Molecular Basis of Enhanced Activity in Factor VIIa-Trypsin Variants Conveys Insights into Tissue Factor-mediated Allosteric Regulation of Factor VIIa Activity.The Journal of biological chemistry · 2016Article
- Sites involved in intra- and interdomain allostery associated with the activation of factor VIIa pinpointed by hydrogen-deuterium exchange and electron transfer dissociation mass spectrometry.The Journal of biological chemistry · 2014Article
- The length of the linker between the epidermal growth factor-like domains in factor VIIa is critical for a productive interaction with tissue factor.Protein science : a publication of the Protein Society · 2014Article
- Mechanism of the Ca2+-induced enhancement of the intrinsic factor VIIa activity.The Journal of biological chemistry · 2008Article
- Essential role of platelet activation via protease activated receptor 4 in tissue factor-initiated inflammation.Arthritis research & therapy · 2008Article
- A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation.Protein science : a publication of the Protein Society · 2007Article
- Augmented intrinsic activity of Factor VIIa by replacement of residues 305, 314, 337 and 374: evidence of two unique mutational mechanisms of activity enhancement.The Biochemical journal · 2004Article
- Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Spin and fluorescent probing of the binding interface between tissue factor and factor VIIa at multiple sites.Biophysical journal · 2001Article
- Binding of Zn2+ to a Ca2+ loop allosterically attenuates the activity of factor VIIa and reduces its affinity for tissue factor.Protein science : a publication of the Protein Society · 2000Article
- Properties of spin and fluorescent labels at a receptor-ligand interface.Biophysical journal · 1999Article
- Structure of human factor VIIa and its implications for the triggering of blood coagulation.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Factor VIIa (fVIIa) is composed of four discrete domains, a gamma-carboxyglutamic acid (Gla)-containing domain, two epidermal growth factor (EGF)-like domains, and a serine protease domain, all of which appear to be involved, to different extents, in an optimal interaction with tissue factor (TF). All except the second EGF-like domain contain at least one Ca2+ binding site and many properties of fVIIa, e.g., TF and phospholipid binding and amidolytic activity, are Ca(2+)-dependent. A CD study was performed to characterize and locate the conformational changes in fVIIa induced by Ca2+ and TF binding. In addition to intact fVIIa, derivatives lacking the Gla domain or the protease domain were used. Assignment of the Ca(2+)-induced changes in the far-UV region of the fVIIa spectrum to the Gla domain could be made by comparing the CD spectra obtained with these fVIIa derivatives. The changes primarily appeared to reflect a Ca(2+)-induced ordering of alpha-helices existing in the apo state of fVIIa. This was corroborated by models of the apo and Ca2+ forms of fVIIa, obtained as difference spectra between fVIIa derivatives, were very similar to those of isolated Gla peptides from other vitamin K-dependent plasma proteins. The near-UV CD spectrum of fVIIa was dominated by aromatic residues residing in the protease domain and specific bands affected by Ca2+ were indicative of tertiary structural alterations. The formation of a fVIIa:TF complex led to secondary structural changes that appeared to be restricted to the catalytic domain, possibly shedding light on the mechanism by which TF induces an enhancement of fVIIa catalytic activity.
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