Abstract：
:Factor X circulates as a serine protease which is converted to the active form at the point of convergence of the intrinsic and extrinsic coagulation pathways. Subsequently, the enzymatic species, factor Xa, is involved in macromolecular complex formation with its cofactor factor Va, a phospholipid surface and calcium to convert prothrombin into thrombin. The gene encoding factor X shares a number of structural and organisational features in common with the other vitamin K-dependent coagulation proteins, suggesting that they have evolved from a common ancestral gene. Each of the exons encoding these proteins can be considered as a module coding for a homologous domain in each protein. These structural domains in factor X are responsible for specific functional properties including gamma-carboxylase recognition, calcium binding, phospholipid surface interaction, as well as cofactor and substrate binding. Studies of recombinant proteins and proteolytic fragments continue to provide significant insight into structure-function relationships of the protein modules within factor X.
journal_name
Blood Revjournal_title
Blood reviewsauthors
Hertzberg Mdoi
10.1016/0268-960x(94)90007-8subject
Has Abstractpub_date
1994-03-01 00:00:00pages
56-62issue
1eissn
0268-960Xissn
1532-1681pii
0268-960X(94)90007-8journal_volume
8pub_type
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