Factor VIIa: Difference between revisions
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[[Factor VIIa]] (FVIIa) is a single chain trypsin-like serine protease [http://en.wikipedia.org/wiki/Serine_protease](EC 3.4.21.21) of 406 residues. The FVII[http://en.wikipedia.org/wiki/Factor_VIIa] zymogen is a glycoprotein consisting of an amino-terminal (N-linked) γ-carboxyglutamic acid (Gla)[http://en.wikipedia.org/wiki/Carboxyglutamic_acid]domain followed by two epidermal growth factor-like (EGF1 and EGF2) domains, a short linker peptide, and a carboxy terminal serine protease domain<ref>PMID:10430872</ref>. The active form, FVIIa, is generated by a specific cleavage of a peptide bond between Arg152 and Ile153 at the end of the linker peptide by either factor Xa (FXa) or thrombin (IIa). This cleavage generates an N-terminal light chain of 152 residues linked to a heavy chain of 254 residues by a disulfide bridge <ref>PMID:6778860</ref>. Following cleavage the newly formed N-terminal inserts itself into a cavity, or the activation pocket, forming a salt bridge with Asp343 (Asp194 trypsin numbering).Formation of this salt bridge allows for the maturation of FVIIa to its active form. The images correspond to one representative Factor VIIa, ''i.e.'' the crystal structure of Human factor VIIa complex with tissue factor and a peptide inhibitor ([[1dan]]). | [[Factor VIIa]] (FVIIa) is a single chain trypsin-like serine protease [http://en.wikipedia.org/wiki/Serine_protease](EC 3.4.21.21) of 406 residues. The FVII[http://en.wikipedia.org/wiki/Factor_VIIa] zymogen is a glycoprotein consisting of an amino-terminal (N-linked) γ-carboxyglutamic acid (Gla)[http://en.wikipedia.org/wiki/Carboxyglutamic_acid]domain followed by two epidermal growth factor-like (EGF1 and EGF2) domains, a short linker peptide, and a carboxy terminal serine protease domain<ref>PMID:10430872</ref>. The active form, FVIIa, is generated by a specific cleavage of a peptide bond between Arg152 and Ile153 at the end of the linker peptide by either factor Xa (FXa) or thrombin (IIa). This cleavage generates an N-terminal light chain of 152 residues linked to a heavy chain of 254 residues by a disulfide bridge <ref>PMID:6778860</ref>. Following cleavage the newly formed N-terminal inserts itself into a cavity, or the activation pocket, forming a salt bridge with Asp343 (Asp194 trypsin numbering).Formation of this salt bridge allows for the maturation of FVIIa to its active form. The images correspond to one representative Factor VIIa, ''i.e.'' the crystal structure of Human factor VIIa complex with tissue factor and a peptide inhibitor ([[1dan]]). | ||
<scene name='39/399790/Cv/3'>Human factor VIIa heavy chain and light chain</scene> | <scene name='39/399790/Cv/3'>Human factor VIIa heavy chain and light chain</scene> complex with <scene name='39/399790/Cv/4'>soluble tissue factor, chains T and U</scene>. | ||
==FVIIa mechanism== | ==FVIIa mechanism== | ||
===General=== | ===General=== | ||