Sandbox Reserved 350: Difference between revisions

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Functionality of Human Coagulation Factor V (FV), as most proteins is strongly correlated to the conformation of the overall strcture. As noted above in the structural section, two structural forms of Human Coagulation Factor V were crystallized. These two structures were disctinct from each other based on a conformational change present ~~in the C2 domain~~, alternating between Open and Closed. This change from close to open by exposing this groove results due to the kind of environment Human Coagulation Factor V finds itself in, and ultimately the source of it's function. This confers that FV is not an enzymatically active protein, but instead acts a cofactor part of the larger Cougulation Cascade ~~(Ref Wiki)~~.

Functionality of Human Coagulation Factor V (FV), as most proteins is strongly correlated to the conformation of the overall strcture. As noted above in the structural section, two structural forms of Human Coagulation Factor V C2 Domain were crystallized. These two structures were disctinct from each other based on a conformational change present, alternating between what was described as a Open and Closed form. This change from close to open by exposing this groove results due to the kind of environment Human Coagulation Factor V finds itself in, and ultimately the source of it's function. This confers that FV is not an enzymatically active protein, but instead acts a cofactor part of the larger [http://en.wikipedia.org/wiki/File:Coagulation_full.svg Cougulation Cascade.]

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The role of Human Coagulation Factor V, is act as a cofactor, enhances the ability of factor Xa to generate from prothrombin once activated (Fva). It is known that FV is activated in a positive feedback mechanism by α-thrombin and aided in conjunction with Human Coagulation Factor Xa, and inhibited by [http://en.wikipedia.org/wiki/Protein_C Active Protein C] [http://www.proteopedia.org/wiki/index.php/1aut (1aut)].

Sandbox Reserved 350: Difference between revisions

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-Functionality of Human Coagulation Factor V (FV), as most proteins is strongly correlated to the conformation of the overall strcture.  As noted above in the structural section, two structural forms of Human Coagulation Factor V were crystallized.  These two structures were disctinct from each other based on a conformational change present in the C2 domain, alternating between Open and Closed.  This change from close to open by exposing this groove results due to the kind of environment Human Coagulation Factor V finds itself in, and ultimately the source of it's function.  This confers that FV is not an enzymatically active protein, but instead acts a cofactor part of the larger Cougulation Cascade (Ref Wiki).
+Functionality of Human Coagulation Factor V (FV), as most proteins is strongly correlated to the conformation of the overall strcture.  As noted above in the structural section, two structural forms of Human Coagulation Factor V C2 Domain were crystallized.  These two structures were disctinct from each other based on a conformational change present, alternating between what was described as a Open and Closed form.  This change from close to open by exposing this groove results due to the kind of environment Human Coagulation Factor V finds itself in, and ultimately the source of it's function.  This confers that FV is not an enzymatically active protein, but instead acts a cofactor part of the larger [http://en.wikipedia.org/wiki/File:Coagulation_full.svg Cougulation Cascade.]
 <br />
 The role of Human Coagulation Factor V, is act as a cofactor, enhances the ability of factor Xa to generate  from prothrombin once activated (Fva).  It is known that FV is activated in a positive feedback mechanism by α-thrombin and aided in conjunction with Human Coagulation Factor Xa, and inhibited by [http://en.wikipedia.org/wiki/Protein_C Active Protein C] [http://www.proteopedia.org/wiki/index.php/1aut (1aut)].