Fibrinogen: Difference between revisions

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[[Image:3hus2.jpg|left|300px|thumb|Crystal Structure of Fibrinogen with peptide ligand, [[3hus]]]]
<StructureSection load='1n73' size='350' side='right' scene='41/410324/Cv/1' caption='Crystal structure of glycosylated fibrinogen fragment D.  Subunit α (green and yellow), β (green and magenta), γ (pink and cyan) complex with the peptide ligand Gly-His-Arg-Pro-amide (red, wheat, blue, black) and Ca+2 ion (PDB code [[1n73]]) '>


<applet load='3hus2.pdb' size='300' frame='true' align='right' scene="Fibrinogen/Starting_scene/1" caption= 'Crystal structure of fibrinogen fragment D with the peptide ligand Gly-Pro-Arg-Pro-amide, [[3hus]]' />
== Function ==


'''Fibrinogen''' is a glycoprotein found in the blood that is converted into fibrin during blood coagulation. Fibrinogen is cleaved by another protein, [[thrombin]], exposing knobs A and B to form fibrin. <ref>PMID:16689770</ref> It is this fibrin that forms clots to prevent excessive bleeding from wounds sustained. Clotting factors, like factor XIII, are often linked to fibrin. <ref>PMID:18673233</ref>
'''Fibrinogen''' is a glycoprotein found in the blood that is converted into fibrin during blood coagulation. Fibrinogen is cleaved by another protein, [[thrombin]], exposing knobs A and B to form fibrin. <ref>PMID:16689770</ref> The fibrin forms clots to prevent excessive bleeding from wounds sustained. Clotting factors, like factor XIII, are often linked to fibrin. <ref>PMID:18673233</ref>


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==3D Printed Physical Model of Fibrinogen==
<br clear="all" />
 
Shown below is a 3D printed physical model of Fibrinogen. The structure is shown as an alpha carbon backbone colored by chain, with the three chains of each copy of fibrinogen colored yellow, blue and purple.
 
[[Image:fibrinogen1_centerForBioMolecularModeling.jpg|550px]]
 
 
====The MSOE Center for BioMolecular Modeling====
 
[[Image:CbmUniversityLogo.jpg | left | 150px]]
 
The [http://cbm.msoe.edu MSOE Center for BioMolecular Modeling] uses 3D printing technology to create physical models of protein and molecular structures, making the invisible molecular world more tangible and comprehensible. To view more protein structure models, visit our [http://cbm.msoe.edu/educationalmedia/modelgallery/ Model Gallery].
 
 
== Structural insights ==
 
Fibrinogen is composed of 2 copies each of 3 non-identical chains α, β, γ (<scene name='Fibrinogen/Fba/1'>Fba</scene>, <scene name='Fibrinogen/Fbb/1'>Fbb</scene>, <scene name='Fibrinogen/Fbg/1'>Fbg</scene>). 
</StructureSection>


==3D Structure of Fibrinogen==
==3D Structure of Fibrinogen==


Fibrinogen is composed of 2 copies each of 3 non-identical chains alpha, beta, gamma (<scene name='Fibrinogen/Fba/1'>Fba</scene>, <scene name='Fibrinogen/Fbb/1'>Fbb</scene>, <scene name='Fibrinogen/Fbg/1'>Fbg</scene>). 
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
{{#tree:id=OrganizedByTopic|openlevels=0|
===Fibrinogen alpha+beta+gamma chains===


==== Human ====
*Fibrinogen α+β+γ chains
hFba + hFbb + hFbg:
[[1re4]], [[1rf0]], [[1n8e]], [[1lt9]]
<br />
hFba + hFbb + hFbg + knobs A & B:
[[3ghg]], [[2q9i]], [[2z4e]]
<br />
hFba + hFbb + hFbg + peptide ligand:
[[3hus]], [[3h32]], [[3e1i]], [[3bvh]], [[2hlo]], [[2hod]], [[2hpc]], [[2oyh]], [[2oyi]], [[2h43]], [[2ffd]], [[1re3]], [[1rf1]], [[1n86]], [[1ltj]]
<br />
hFba + hFbb + hFbg + thrombin + PPACK thrombin inhibitor:
[[2a45]]
==== Cow ====
cFba + cFbb + cFbg:
[[1jy3]], [[1deq]]<br />
cFba+cFbb+cFbg proteolytic fragment: [[1jy2]]
==== Sea lamprey ====
Fba + Fbb + Fbg + peptide ligand:
[[1n73]], [[1lwu]]
==== Hen ====
heFba + heFbb + heFbg:
[[1ei3]]
<br />
heFba + heFbb + heFbg + peptide ligand:
[[1m1j]]


===Fibrinogen alpha chain===
**[[3hus]], [[3h32]], [[3e1i]], [[3bvh]], [[2hlo]], [[2hod]], [[2hpc]], [[2oyh]], [[2oyi]], [[2h43]], [[2ffd]], [[1re3]], [[1rf1]], [[1n86]], [[1ltj]] – hFba+hFbb+hFbg+peptide ligand – human<br />
**[[3ghg]], [[2q9i]], [[2z4e]] - hFba+hFbb+hFbg+knob A & B<br />
**[[2xnx]], [[2xny]] - hFba+hFbb+hFbg + M1 protein<br />
**[[2a45]] - hFba+hFbb+hFbg+thrombin+PPACK thrombin inhibitor<br />
**[[1re4]], [[1rf0]], [[1n8e]], [[1lt9]] - hFba+hFbb+hFbg<br />
**[[1jy3]], [[1deq]] – bFba+Fbb+Fbg – bovine<br />
**[[1jy2]] - bFba+Fbb+Fbg proteolytic fragment<br />
**[[1m1j]] - cFba+Fbb+Fbg+peptide ligand – chicken<br />
**[[1ei3]] - cFba+Fbb+Fbg<br />
**[[1n73]], [[1lwu]] - Fba+Fbb+Fbg+peptide ligand – Sea lamprey<br />


cFba: [[2baf]]<br />
*Fibrinogen α chain
cFba – NMR: [[2jor]]<br />
hFba EC domain: [[1fzd]] <br />


===Fibrinogen beta chain===
**[[1fzd]] – hFba EC domain<br />
**[[1bbr]] – hFba+cε-thrombin<br />
**[[2jor]] – bFba – NMR<br />
**[[2baf]] – bFba<br />


hFb fragment D: [[1fze]], [[1fza]], [[1fzb]]<br />
*Fibrinogen β chain
hFb fragment double-D + peptide ligand: [[1fzf]], [[1fzg]]<br />


===Fibrinogen gamma chain===
**[[1fzf]], [[1fzg]] – hFb fragment double-D +peptide ligand<br />
**[[1fze]], [[1fza]], [[1fzb]] – hFb fragment D<br />


hFbg: [[1fic]], [[1fid]] <br />
*Fibrinogen γ chain
hFbg + Ca: [[1fib]]<br />
hFbg + peptide ligand: [[2fib]], [[3fib]] <br />
hFbg + SaClumping Factor A – ''Staphylococcus aureus'': [[2vr3]]<br />
hFbg + Integrin alpha IIB + Integrin beta-3 + Monoclonal antibody heavy and light chains: [[2vdo]], [[2vdp]], [[2vdq]], [[2vdr]] <br />


**[[1fic]], [[1fid]] – hFbg<br />
**[[3fib]] – hFbg C terminal<br />
**[[2vr3]] – hFbg+SaClumping Factor A – ''Staphylococcus aureus''<br />
**[[2vdo]], [[2vdp]], [[2vdq]], [[2vdr]] – hFbg+Integrin alpha IIB+Integrin beta-3+ antibody <br />
**[[2fib]], [[3fib]] - hFbg+peptide ligand<br />
**[[1fib]] – hFbg+Ca<br />
**[[2hwl]] – hFbg peptide+prothrombin<br />
**[[2y7l]] – hFbg + agglutinin-like protein <br />
**[[1dug]] – Fbg C-terminal/glutathione S-transferase – ''Schistosoma japonicum''<br />
}}
==References==
==References==
<references />
<references />


[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

David Canner, Angel Herraez, Alexander Berchansky, Michal Harel, Mark Hoelzer