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Literature summary for 3.4.21.21 extracted from
- A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation (2007), Protein Sci., 16, 671-682.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| tissue factor | required to attain full catalytic competency and to initiate blood coagulation, mechanism of TF allosterical activation of FVIIa, structural dynamics approach that combines molecular dynamics simulations and hydrogen/deuterium exchange mass spectrometry on free and TF-bound FVIIa, TF structures involved are activation loop 3 residues 365-374/216-225 of the so-called activation domain and the 170-loop residues 313-322/170A-175, overview | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | N-glycosylation at Asn322, rapid deglycosylation by PNGase F | Homo sapiens |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | structure modeling, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| factor VIIa | - |
Homo sapiens |
| FVIIa | - |
Homo sapiens |
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