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| - | <StructureSection load='1n73' size='350' side='right' scene='Fibrin/Cv/2' caption='Fibrin α1 subunit (red, yellow), β subunit (Green, blue), γ subunit (orange, magenta) from Petromyzon marinus (PDB entry [[1n73]]'> | + | <StructureSection load='1n73' size='350' side='right' scene='41/417472/Cv/3' caption='Fibrin α1 subunit (red, yellow), β subunit (cyan, blue), γ subunit (orange, magenta) from Petromyzon marinus (PDB entry [[1n73]])'> |
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| | == Function == | | == Function == |
Revision as of 09:32, 21 February 2016
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Function
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)[1].
Disease
Overexpression of FIa can cause thrombosis.
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3D Structures of Fibrin
Updated on 21-February-2016
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
References
- ↑ Yang Z, Pandi L, Doolittle RF. The crystal structure of fragment double-D from cross-linked lamprey fibrin reveals isopeptide linkages across an unexpected D-D interface. Biochemistry. 2002 Dec 31;41(52):15610-7. PMID:12501189
