Factor VIIa: Difference between revisions

{{STRUCTURE_1dan| PDB=1dan| SCENE= }}

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.