Effect of Ca2+ on the structure of vitamin K-dependent coagulation factors.
Coagulation factors VII, IX, X, and protein C contain an N-terminal module with 9-12 gamma-carboxyglutamic acid (Gla) residues. It is followed by two modules that are homologous to the epidermal growth factor (EGF) and a C-terminal serine protease module. Upon calcium binding to the Gla module the side chains of three hydrophobic residues are exposed in a manner indicating that they interact with biological membranes. The calcium-binding site in the first EGF-like module appears to be required for proper orientation of the Gla and EGF-like modules relative to each other. A single calcium-binding site is also present in the serine protease module. The properties of these calcium-binding sites are briefly reviewed.
Department of Physical Chemistry 2, Lund University, Malmo, Sweden.
M
M
Sunnerhagen
T
T
Drakenberg
S
S
Forsen
J
J
Stenflo
D000595:Amino Acid Sequence; D001665:Binding Sites; D001779:Blood Coagulation Factors / Q000737:chemistry*; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D004815:Epidermal Growth Factor / Q000737:chemistry; D016326:Extracellular Matrix Proteins; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011486:Protein C / Q000737:chemistry*; D000097568:Matrix Gla Protein
D001779:Blood Coagulation Factors; D002135:Calcium-Binding Proteins; D004815:Epidermal Growth Factor; D016326:Extracellular Matrix Proteins; D011486:Protein C; D000097568:Matrix Gla Protein