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From Proteopedia
| This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543. |
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Integrin αIIbβ3 (2VDL)
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 ligand binding and transduction of the activation signal. 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.
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
