Interaction of integrin alphaIIb beta3 with Fibrinogen

Stable Identifier
Reaction [binding]
Homo sapiens
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The overall shape of integrins is that of a globular 'head' supported by two rod like legs. The ligand-binding pocket is formed by the combination of A-domain or beta-I domain on the beta3 subunit and the putative beta-propeller fold on the alphaIIb subunit in the head regions. The binding of ligand to integrin is also dependent on divalent cations (usually Mn++ or Mg++or Ca++). A conserved motif, the metal ion-dependant adhesion site (MIDAS) is located in the alpha and the beta chains that coordinate the divalent cation at the top of the domain.
Active integrin alphaIIb beta3 interacts with a variety of plasma proteins such as fibrinogen, vWF, thrombin, thrombospondin, and fibronectin. The ability of alphaIIbbeta3 to bind fibrinogen plays a crucial role in platelet aggregation and hemostasis. Most of these matrix proteins have integrin binding sites of 3-6 amino acids length, of which the best known are the 'RGD' and 'KGD' motifs. The alpha and beta integrin subunits are both required for ligand binding.
Literature References
PubMed ID Title Journal Year
16040750 Multi-step fibrinogen binding to the integrin (alpha)IIb(beta)3 detected using force spectroscopy

Litvinov, RI, Shuman, H, Weisel, JW, Bennett, JS

Biophys J 2005
10446041 Integrin signaling

Ruoslahti, E, Giancotti, FG

Science 1999
14754902 Integrin activation

Calderwood, DA

J Cell Sci 2004
Orthologous Events
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