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| ==Fibrinogen 3GHG == | | ==Your Heading Here (maybe something like 'Structure')== |
| <StructureSection load='3GHG' size='340' side='right' caption='Caption for this structure' scene='78/781216/Origfibri/1''> | | <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. |
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| == Structure ==
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| Fibrinogen is located in the circulatory system as part of plasma, it is readily available.
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| 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.
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| == 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.
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| == 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
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| | == Relevance == |
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| == Structural highlights == | | == Structural highlights == |
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| <scene name='78/781216/Abysubunitsrbg/5'>three non-identical chains</scene>
| | 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. |
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| <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.
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| </StructureSection> | | </StructureSection> |
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| == References == | | == References == |
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| 1. Acharya, S. S., & Dimichele, D. M. (2008). Rare inherited disorders of fibrinogen. Haemophilia, 14(6), 1151–1158. doi: 10.1111/j.1365-2516.2008.01831.x
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| 2. Al-Hussaini, A., Altalhi, A., Hag, I. E., Alhussaini, H., Francalanci, P., Giovannoni, I., & Callea, F. (2014). Hepatic fibrinogen storage disease due to the fibrinogen γ375 Arg → Trp mutation "fibrinogen aguadilla" is present in Arabs. Saudi Journal of Gastroenterology, 20(4), 255. doi: 10.4103/1319-3767.136985
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| 3. Doolittle, R., Kollman, J., Sawaya, M., Pandi, L., & Riley, M. (2009). Crystal Structure of Human Fibrinogen. American Chemical Society. doi: 10.2210/pdb3ghg/pdb
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| 4. Köhler, S., Schmid, F., & Settanni, G. (2015). The Internal Dynamics of Fibrinogen and Its Implications for Coagulation and Adsorption. PLOS Computational Biology, 11(9). doi: 10.1371/journal.pcbi.1004346
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| 5. Medved, L., & Weisel, J. W. (2009). Recommendations for nomenclature on fibrinogen and fibrin. Journal of Thrombosis and Haemostasis, 7(2), 355–359. doi: 10.1111/j.1538-7836.2008.03242.x
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