Protein Domain : IPR012290

Type:  Domain Name:  Fibrinogen, alpha/beta/gamma chain, coiled coil domain
Description:  Fibrinogen plays key roles in both blood clotting and platelet aggregation. During blood clot formation, the conversion of soluble fibrinogen to insoluble fibrin is triggered by thrombin, resulting in the polymerisation of fibrin, which forms a soft clot; this is then converted to a hard clot by factor XIIIA, which cross-links fibrin molecules. Platelet aggregation involves the binding of the platelet protein receptor integrin alpha(IIb)-beta(3) to the C-terminal D domain of fibrinogen []. In addition to platelet aggregation, platelet-fibrinogen interaction mediates both adhesion and fibrin clot retraction. Fibrinogen occurs as a dimer, where each monomer is composed of three non-identical chains, alpha, beta and gamma, linked together by several disulphide bonds []. The N-terminals of all six chains come together to form the centre of the molecule (E domain), from which the monomers extend in opposite directions as coiled coils, followed by C-terminal globular domains (D domains). Therefore, the domain composition is: D-coil-E-coil-D. At each end, the C-terminal of the alpha chain extends beyond the D domain as a protuberance that is important for cross-linking the molecule. During clot formation, the N-terminal fragments of the alpha and beta chains (within the E domain) in fibrinogen are cleaved by thrombin, releasing fibrinopeptides A and B, respectively, and producing fibrin. This cleavage results in the exposure of four binding sites on the E domain, each of which can bind to a D domain from different fibrin molecules. The binding of fibrin molecules produces a polymer consisting of a lattice network of fibrins that form a long, branching, flexible fibre [, ]. Fibrin fibres interact with platelets to increase the size of the clot, as well as with several different proteins and cells, thereby promoting the inflammatory response and concentrating the cells required for wound repair at the site of damage.This entry represents the coiled-coil domain and part of the N-terminal E domain found in all three fibrinogen polypeptides, namely the alpha, beta and gamma chains. Short Name:  Fibrinogen_a/b/g_coil_dom
Paste the following link

0 Child Features

0 Contains

1 Cross References

Identifier
PF08702

0 Found In

6 GO Annotations

GO Term Gene Name
GO:0005102 IPR012290
GO:0030674 IPR012290
GO:0007165 IPR012290
GO:0030168 IPR012290
GO:0051258 IPR012290
GO:0005577 IPR012290

6 Ontology Annotations

GO Term Gene Name
GO:0005102 IPR012290
GO:0030674 IPR012290
GO:0007165 IPR012290
GO:0030168 IPR012290
GO:0051258 IPR012290
GO:0005577 IPR012290

0 Parent Features

4 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
SapurV1A.1209s0070.1.p PAC:31410624 Salix purpurea 269  
AUR62009108-RA PAC:36297171 Chenopodium quinoa 1270  
AUR62020559-RA PAC:36283056 Chenopodium quinoa 1207  
AUR62020563-RA PAC:36282999 Chenopodium quinoa 1207  

4 Publications

First Author Title Year Journal Volume Pages PubMed ID
            12799374
            11460466
            11593005
            15837518