Lauren Ferris/Sandbox 1
From Proteopedia
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| - | <Structure load='1aut' size='400' color='white' frame='true' align='right' caption='pdb: 1AUT' scene='Lauren_Ferris/Sandbox_1/All/1'> | + | <Structure load='1aut' size='400' color='white' frame='true' align='right' caption='pdb: 1AUT' scene='Lauren_Ferris/Sandbox_1/All/1'> |
===Structure=== | ===Structure=== | ||
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The serine protease domain, is composed of Histidine 211, Aspartic Acid 257, and Serine 360. The serine protease domain is part of the heavy chain. | The serine protease domain, is composed of Histidine 211, Aspartic Acid 257, and Serine 360. The serine protease domain is part of the heavy chain. | ||
| - | Other key structural features of the 3-Dimensional structure include a cluster of positive charges at the surface of activated protein c near the active site. These positive charges are thought to bind to substrates and inhibitors. | + | Other key structural features of the 3-Dimensional structure include a cluster of positive charges at the surface of activated protein c near the active site. These positive charges are thought to bind to substrates and inhibitors. </scene> |
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Revision as of 01:47, 15 May 2012
Activated Protein C
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Introduction
The vitamin K dependent zymogen Protein C is an integral component of the blood coagulation system. The blood coagulation system is composed of two pathways that converge to form the prothrombinase complex (FVa-FXa). Thrombin is generated from this complex and catalyzes the formation of the clot by activating Fibrinogen and FXIII. Thrombin will also bind to thrombomodulin and the complex removes 12 peptides(Arg169-Leu170) from the protein, converting the protein to the active form: Activated Protein C.[1][2][3] Activated Protein C will function as a down-regulator of procoagulant stimuli through the degradation of zymogens and their active counterparts: FV/FVa and FVIII/FVIIIa. [4][5] This ability enables Protein C to modulate the coagulant response, preventing unchecked clotting.
Protein C has also been recognized for its role in anti-inflammatory and cytoprotective signaling responses in endothelial cells. Protein C will bind to an endothelial protein c receptor (EPCR) and then activate protease-activated receptor (PAR-1).[6]
Protein C is synthesized in the liver and circulates the blood at a concentration of 4 ug/mL. The liver conformation is a single polypeptide sequence with an additional 42 amino acids attached at the N-terminus. This structure is known as the pre-pro sequence. Subsequent removal of these peptides as well as Lys156-Arg157 will result in the 62 kD protein that is often observed.[7]
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