Big rigs in blood coagulation

Article Abstract:

A study dealing with the characterization of the two major participants in blood clotting process was able to shed light on how the process is initiated. The two components are the tissue factor (TF) and coagulation factor VIIa (FVIIa). The crystal structure obtained in the study was able to give a picture of the workings of TF and FVIIa. TF was shown to serve as a useful apparatus for FVIIa. It prevented movement and bound the protein enzyme to the active site thereby playing a major role in initiating the generation of fibrin from plasma fibrinogen, an intial step in blood coagulation.

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The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor

Article Abstract:

The crystal structure of the complex of blood coagulation factor VIIa (FVIIa) with tissue factor (TF) is presented using collected data from a single large crystal at applied resolutions of up to 2.0 angstroms. The structure was solved by molecular replacement of a thrombin-based model and coordinates of soluble TF. It is observed from the structure that FVIIA has four defined areas and an extended spatial arrangement. This explains the initial step in blood coagulation which is triggered by the positional binding of tissue factor to FVIIa at three active sites.

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Not just an active site

Article Abstract:

New insights into the structure, function and medical importance of exosites in enzymes involved in blood-clotting are provided.

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