Fibrin

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{{STRUCTURE_1n73| PDB=1n73 | SIZE=400| SCENE=Fibrin/Cv/2 |right|CAPTION=Fibrin α1 subunit (red, yellow), β subunit (Green, blue), γ subunit (orange, magenta) from ''Petromyzon marinus'', [[1n73]] }}
{{STRUCTURE_1n73| PDB=1n73 | SIZE=400| SCENE=Fibrin/Cv/2 |right|CAPTION=Fibrin α1 subunit (red, yellow), β subunit (Green, blue), γ subunit (orange, magenta) from ''Petromyzon marinus'', [[1n73]] }}
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[[Fibrin]] (or Factor Ia, FIa) is a fibrous protein which when polymerized is involved in blood clotting. The polymerization epitopes of FIa are called A-knob and B-knob. [[Fibrinogen]] (Factor I, FI) is converted by thrombin to fibrin. Limited proteolysis of FI results in a fragment named D which when cross-linked by factor XIII is called double-D FIa (DDFIa). The images at the left and at the right correspond to one representative Fibrin, ''i.e.'' the crystal structure of Fibrin from ''Petromyzon marinus'' ([[1n73]]).
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[[Fibrin]] (or Factor Ia, FIa) is a fibrous protein which when polymerized is involved in blood clotting. The polymerization epitopes of FIa are called A-knob and B-knob. [[Fibrinogen]] (Factor I, FI) is converted by thrombin to fibrin. Limited proteolysis of FI results in a fragment named D which when cross-linked by factor XIII is called double-D FIa (DDFIa).
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Revision as of 08:18, 27 August 2014

Template:STRUCTURE 1n73

Fibrin (or Factor Ia, FIa) is a fibrous protein which when polymerized is involved in blood clotting. The polymerization epitopes of FIa are called A-knob and B-knob. Fibrinogen (Factor I, FI) is converted by thrombin to fibrin. Limited proteolysis of FI results in a fragment named D which when cross-linked by factor XIII is called double-D FIa (DDFIa).

Contents

3D Structures of Fibrin

Updated on 27-August-2014

3h32 – hFIa peptide+ hFI α, β, γ chains – human
2q9i, 2z4e - hFIa B-knob+ hFI α, β, γ chains
2hlo, 1n86 - hFIa α, β, γ chains + peptide
1n8e - hFIa α, β, γ chains
1n73 - FIa α, β, γ chains + peptide – Sea lamprey
1fzc – hDDFIa+peptide

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel

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