Sandbox Reserved 596: Difference between revisions
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'''Structure''' | '''Structure''' | ||
<Structure load='3H5C' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | |||
PZ is a single-chain protein with a N-terminal domain rich in γ-carboxyglutamic acids (Gla), two epidermal growth factor-like (EGF) domains and a C-terminal serine protease-like domain and has a molecular weight of 62 kDa. PZ genetically and structurally mimics other factors of the coagulation cascade but it is not a catalyticaly active enzyme. PZ is not like the other vitamin k-dependent coagulation factors because it does not have an active center, thus it lacks the Ser (S195) and His (H57) of the catalytic triad needed for the active site of serine proteases, like the coagulation factors VII, IX, X, and protein C. PZ's 390 amino acid sequence is N-terminally analogous to the serine protease coagulation factors, whose similarly composed genes are found clustered together along with PROZ on chromosome 13. PZ is 33% homologous in amino acid sequence to the coagulation factor it aids in inhibiting, factor Xa (FXa). PZ's binding interface is similar to that of thrombin, an anionic heparin binding site named exocite II. | PZ is a single-chain protein with a N-terminal domain rich in γ-carboxyglutamic acids (Gla), two epidermal growth factor-like (EGF) domains and a C-terminal serine protease-like domain and has a molecular weight of 62 kDa. PZ genetically and structurally mimics other factors of the coagulation cascade but it is not a catalyticaly active enzyme. PZ is not like the other vitamin k-dependent coagulation factors because it does not have an active center, thus it lacks the Ser (S195) and His (H57) of the catalytic triad needed for the active site of serine proteases, like the coagulation factors VII, IX, X, and protein C. PZ's 390 amino acid sequence is N-terminally analogous to the serine protease coagulation factors, whose similarly composed genes are found clustered together along with PROZ on chromosome 13. PZ is 33% homologous in amino acid sequence to the coagulation factor it aids in inhibiting, factor Xa (FXa). PZ's binding interface is similar to that of thrombin, an anionic heparin binding site named exocite II. | ||
