ArticleProceedings of the National Academy of Sciences of the United States of America1999
Structure of human factor VIIa and its implications for the triggering of blood coagulation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Antioxidant role of methionine-containing intra- and extracellular proteins.Biophysical reviews · 2023Review
- A thrombophilic allele of clotting Factor VII/VIIa promoting recurrent pulmonary emboli, clinical details, and a structural model of the altered protein: a case report.Journal of medical case reports · 2023Article
- 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
- Uncovering Membrane-Bound Models of Coagulation Factors by Combined Experimental and Computational Approaches.Thrombosis and haemostasis · 2021Review
- Article
- Alcohol functionality in the fatty acid backbone of sphingomyelin guides the inhibition of blood coagulation.RSC advances · 2021Article
- Characterization of the inhibition mechanism of a tissuefactor inhibiting single-chain variable fragment: a combined computational approach.Journal of molecular modeling · 2020Article
- Pre- and post-docking sampling of conformational changes using ClustENM and HADDOCK for protein-protein and protein-DNA systems.Proteins · 2020Article
- Coagulation factors VII, IX and X are effective antibacterial proteins against drug-resistant Gram-negative bacteria.Cell research · 2019Article
- Crystal structure, epitope, and functional impact of an antibody against a superactive FVIIa provide insights into allosteric mechanism.Research and practice in thrombosis and haemostasis · 2019Article
- Allostery in Coagulation Factor VIIa Revealed by Ensemble Refinement of Crystallographic Structures.Biophysical journal · 2019Article
- Orphan Three-Finger Toxins Bind at Tissue Factor-Factor VIIa Interface to Inhibit Factor X Activation: Identification of Functional Site by Docking.TH open : companion journal to thrombosis and haemostasis · 2018Article
- Evolutionary conservation of the allosteric activation of factor VIIa by tissue factor in lamprey.Journal of thrombosis and haemostasis : JTH · 2018Article
- The "Phagocytic Synapse" and Clearance of Apoptotic Cells.Frontiers in immunology · 2017Review
- 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
- Structure-Function Relationship of the Interaction between Tissue Factor and Factor VIIa.Seminars in thrombosis and hemostasis · 2015Review
- 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
- Structural biology of factor VIIa/tissue factor initiated coagulation.Frontiers in bioscience (Landmark edition) · 2012Review
- Antibody-induced enhancement of factor VIIa activity through distinct allosteric pathways.The Journal of biological chemistry · 2012Article
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Authors and funding
5 authors.
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Abstract
Factor VIIa (EC 3.4.21.21) is a trypsin-like serine protease that plays a key role in the blood coagulation cascade. On injury, factor VIIa forms a complex with its allosteric regulator, tissue factor, and initiates blood clotting. Although the structure of the binary complex has already been determined [Banner, D. W., D'Arcy, A., Chène, C., Winkler, F. K., Guha, A., Konigsberg, W. H., Nemerson, Y. & Kirchhofer, D. (1996) Nature (London) 380, 41-46], the conformational effects of cofactor binding to factor VIIa are not known in detail because of a lack of structural information on free factor VIIa. Here we report the structure of gamma-carboxyglutamic acid-domainless human coagulation factor VIIa at a resolution of 2.8 A. The molecule adopts an extended conformation within the crystal similar to that previously observed for the full-length protein in complex with tissue factor. Detailed comparison of free and tissue factor-bound factor VIIa reveals several structural differences. The binding mode of the active-site inhibitor D-Phe-Phe-Arg methyl ketone differs in the two structures, suggesting a role for the cofactor in substrate recognition. More importantly, a surface-exposed alpha-helix in the protease domain (residues 307-312), which is located at the cofactor recognition site, is distorted in the free form of factor VIIa. This subtle structural difference sheds light on the mechanism of the dramatic tissue factor-induced enhancement of factor VIIa activity.
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