Sandbox GGC14: Difference between revisions

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==Fibrinogen 3GHG ==

~~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 ==

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 ==

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

== Disease ==

Sandbox GGC14: Difference between revisions

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 ==Fibrinogen 3GHG ==
 <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 &lt; and &gt; 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 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 ==
+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
 == Disease ==