Sandbox GGC14: Difference between revisions
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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''> | ||
== Structure == | == Structure == | ||
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 == | ||
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 10:54, 20 November 2019
Fibrinogen 3GHGFibrinogen 3GHG
StructureFibrinogen is a glycoprotein made up of two subunits which include 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. FunctionFibrinogen 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 DiseaseCongenital Afibrinogenemia – a genetic disorder that results in the lack of fibrinogen which causes abnormal bleeding
Structural highlights
This is a sample scene created with SAT to by Group, and another to make 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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ReferencesReferences
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