Sandbox GGC14
From Proteopedia
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==Fibrinogen 3GHG == | ==Fibrinogen 3GHG == | ||
<StructureSection load='3GHG' size='340' side='right' caption='Caption for this structure' scene='78/781216/Origfibri/1''> | <StructureSection load='3GHG' size='340' side='right' caption='Caption for this structure' scene='78/781216/Origfibri/1''> | ||
| - | This is a default text for your page '''Sandbox GGC14'''. 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 == | == Structure == | ||
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Fibrinogen is a 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. | Fibrinogen is a 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 the coagulation, which is initiated through either an instinctive or extinctive pathway. Both pathways trigger a cascade of reactions that lead to coagulation. At some point the protease thrombin is activated, thrombin then converts fibrinogen to fibrin. It does this by cleaving both the fibrinopeptide A and B off of the amino terminus of the alpha and beta chains. The alpha and beta knobs will bind to A and B holes of other fibrin molecules making a fibrin mesh strong enough to hold the platelet plug. | ||
αγβ | αγβ | ||
== Disease == | == Disease == | ||
Revision as of 07:54, 20 November 2019
Fibrinogen 3GHG
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References
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
2. Doolittle, R., Kollman, J., Sawaya, M., Pandi, L., & Riley, M. (2009). Crystal Structure of Human Fibrinogen. American Chemical Society. doi: 10.2210/pdb3ghg/pdb
3. 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
4. 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
