Sandbox Reserved 1493: Difference between revisions
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'''Integrin αIIbβ3''' (or glycoprotein IIb/IIIa) is a complex present on the membrane of platelets that intervenes in the activation, adherence and aggregation of platelets during '''clotting'''. It is a cation-dependant heterodimeric transmembrane receptor containing a large extracellular headpiece and short intracellular tails. It is synthesized in megakaryocytes. | '''Integrin αIIbβ3''' (or glycoprotein IIb/IIIa) is a complex present on the membrane of platelets that intervenes in the activation, adherence and aggregation of platelets during '''clotting'''. It is a cation-dependant heterodimeric transmembrane receptor containing a large extracellular headpiece and short intracellular tails. It is synthesized in megakaryocytes. | ||
Its particular shape and localisation on the membrane allows both transduction of the intracellular activation signal and extracellular ligand binding. It is the dominant integrin on '''platelets''' with 70,000 to 90,000 receptors expressed on each platelet in the resting state. | Its particular shape and localisation on the membrane allows both transduction of the '''intracellular activation signal''' and extracellular '''ligand binding'''. It is the dominant integrin on '''platelets''' with 70,000 to 90,000 receptors expressed on each platelet in the resting state. | ||
The headpiece (2VDL) of integrin αIIbβ3 enables cation-facilitated ligand binding with multiple ligands (most known being [[fibrinogen]], [[fibronectin]], von Willebrand factors, [[thrombospondin]] and vitronectin). Binding affinity is dynamic and depends on the conformational status of the receptor. | The headpiece (2VDL) of integrin αIIbβ3 enables cation-facilitated ligand binding with multiple ligands (most known being [[fibrinogen]], [[fibronectin]], von Willebrand factors, [[thrombospondin]] and vitronectin). Binding affinity is dynamic and depends on the conformational status of the receptor. | ||
