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Sandbox GGC14
From Proteopedia
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| - | == | + | ==Your Heading Here (maybe something like 'Structure')== |
| - | <StructureSection load=' | + | <StructureSection load='3VEV' size='340' side='right' caption='Caption for this structure' scene=''> |
| + | This is a default text for your page. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| + | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
| - | == Structure == | ||
| - | Fibrinogen is located in the circulatory system as part of plasma, it is readily available. | ||
| - | Fibrinogen is a ~340KD glycoprotein made up of two subunits which include <scene name='78/781216/Abysubunitsrbg/5'>three non-identical chains</scene> Aα, Bβ γ. Its central region also called “E region” is where all chains meet, the chains intertwine with each other to hold both of the subunits together. At the ends of the a and b chains are fibrinopeptides, fibrinopeptide A is about 16 amino acids long, while fibrinopeptide B is around 15 amino acids long. These small peptides become very important when activating fibrinogen. On both ends of fibrinogen are the D regions containing the β & γ nodule and the coiled-coil region. | ||
== Function == | == Function == | ||
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| - | Fibrinogen is an essential protein in coagulation, which is initiated through either an intrinsic or extrinsic pathway. Both pathways trigger a cascade of reactions that lead to the formation of a blood clot. At some point the protease thrombin is activated, thrombin then converts fibrinogen to fibrin. It does this by cleaving both the <scene name='78/781216/Fribrinopeptide_a_and_b/3'>fibrinopeptide A and B</scene> off of the amino terminus of the alpha and beta chains. The alpha and beta knobs will bind to <scene name='78/781216/Aandb_modules/1'>a and b holes</scene> of other fibrin molecules making fibrin mesh strong enough to hold the platelet plug. | ||
== Disease == | == Disease == | ||
| - | '''Congenital Afibrinogenemia''' – a genetic disorder that results in the lack of fibrinogen which causes abnormal bleeding including gastrointestinal hemorrhage, cutaneous bleeding, etc. | ||
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| - | '''Hepatic fibrinogen storage disease''' - occurs when there is a mutation in the γ chain which causes the storage of fibrinogen in the ER of liver cells. The storage of fibrinogen in these cells can cause liver disease. | ||
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| - | '''Acquired Dysfibrinogenemia''' - may occur as a result of liver disease which causes an error during fibrinogen synthesis resulting in dysfunctional fibrinogen | ||
| + | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
| - | <scene name= | + | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. |
| - | <scene name='78/781216/Fribrinopeptide_a_and_b/3'>fibrinopeptide A and B</scene> | ||
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| - | <scene name='78/781216/Aandb_modules/1'>a and b holes</scene> | ||
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| - | <scene name='78/781216/Origfibri/1'>Fibrinogen</scene> | ||
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| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
</StructureSection> | </StructureSection> | ||
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== References == | == References == | ||
| - | + | <references/> | |
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Revision as of 15:20, 10 February 2021
Your Heading Here (maybe something like 'Structure')
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
