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]]) '>


== Function ==


{{STRUCTURE_1n73| PDB=1n73  | SIZE=350| SCENE= |right|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,[[1n73]].}}
'''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>


==3D Printed Physical Model of Fibrinogen==


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>
 
 
 
 
 
 
 
 
 
 
 
 
 
 
'''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>
 
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==3D Structure of Fibrinogen==
==3D Structure of Fibrinogen==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|


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>). 
*Fibrinogen α+β+γ chains
 
===Fibrinogen α+β+γ chains===
 
[[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]] – cFba+cFbb+cFbg – cow<br />
[[1jy2]] - cFba+cFbb+cFbg proteolytic fragment<br />
[[1n73]], [[1lwu]] - Fba+Fbb+Fbg+peptide ligand – Sea lamprey<br />
[[1m1j]] - heFba+heFbb+heFbg+peptide ligand – hen<br />
[[1ei3]] - heFba+heFbb+heFbg<br />
 
===Fibrinogen α chain===


[[1fzd]] – hFba EC domain<br />
**[[3hus]], [[3h32]], [[3e1i]], [[3bvh]], [[2hlo]], [[2hod]], [[2hpc]], [[2oyh]], [[2oyi]], [[2h43]], [[2ffd]], [[1re3]], [[1rf1]], [[1n86]], [[1ltj]] – hFba+hFbb+hFbg+peptide ligand – human<br />
[[1bbr]] – hFba+cε-thrombin<br />
**[[3ghg]], [[2q9i]], [[2z4e]] - hFba+hFbb+hFbg+knob A & B<br />
[[2jor]] – cFba – NMR<br />
**[[2xnx]], [[2xny]] - hFba+hFbb+hFbg + M1 protein<br />
[[2baf]] – cFba<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 />


===Fibrinogen β chain===
*Fibrinogen α chain


[[1fzf]], [[1fzg]] – hFb fragment double-D +peptide ligand<br />
**[[1fzd]] – hFba EC domain<br />
[[1fze]], [[1fza]], [[1fzb]] – hFb fragment D<br />
**[[1bbr]] – hFba+cε-thrombin<br />
**[[2jor]] – bFba – NMR<br />
**[[2baf]] – bFba<br />


===Fibrinogen γ chain===
*Fibrinogen β chain


[[2vr3]] – hFbg+SaClumping Factor A – ''Staphylococcus aureus''<br />
**[[1fzf]], [[1fzg]] – hFb fragment double-D +peptide ligand<br />
[[2vdo]], [[2vdp]], [[2vdq]], [[2vdr]] – hFbg+Integrin alpha IIB+Integrin beta-3+Monoclonal antibody heavy and light chains<br />
**[[1fze]], [[1fza]], [[1fzb]] – hFb fragment D<br />
[[2fib]], 3fib - hFbg+peptide ligand<br />
[[1fib]] – hFbg+Ca<br />
[[1fic]], [[1fid]] – hFbg<br />
[[3fib]] – hFbg C terminal<br />
[[1dug]] – Fbg C-terminal/glutathione S-transferase – ''Schistosoma japonicum''<br />
[[2hwl]] – hFbg peptide+prothrombin<br />


*Fibrinogen γ chain


**[[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]]

Latest revision as of 10:16, 28 July 2020


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. [1] The fibrin forms clots to prevent excessive bleeding from wounds sustained. Clotting factors, like factor XIII, are often linked to fibrin. [2]

3D Printed Physical Model of Fibrinogen

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.


The MSOE Center for BioMolecular Modeling

The 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 Model Gallery.


Structural insights

Fibrinogen is composed of 2 copies each of 3 non-identical chains α, β, γ (, , ).

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)

Drag the structure with the mouse to rotate

3D Structure of Fibrinogen3D Structure of Fibrinogen

Updated on 28-July-2020

ReferencesReferences

  1. ↑ Betts L, Merenbloom BK, Lord ST. The structure of fibrinogen fragment D with the 'A' knob peptide GPRVVE. J Thromb Haemost. 2006 May;4(5):1139-41. PMID:16689770 doi:10.1111/j.1538-7836.2006.01902.x
  2. ↑ Muszbek L, Bagoly Z, Bereczky Z, Katona E. The involvement of blood coagulation factor XIII in fibrinolysis and thrombosis. Cardiovasc Hematol Agents Med Chem. 2008 Jul;6(3):190-205. PMID:18673233

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