Sandbox Reserved 1447
From Proteopedia
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== Function == | == Function == | ||
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== Structure == | == Structure == | ||
- | It contains four domains from A-D. The A and B domains contain 3 different domains and C has two domains while D has four. Each domain plays a role in different functions. For example, domains D’ and D3 exhibit binding sites for factor VIII. The structure of VWF was changed from the original thought structure in 1986. The original structure showed to be: D1-D2-D’-D3-A1-A2-A3-D4-B1-B2-B3-C1-C2-CK. However, the new shows the structure is D1-D2-D’-D3-A1-A2-A3-D4-C1-C2-C3-C4-C5-C6-CK. The <scene name='77/778327/A1_domain/1'>A1</scene> domain of VWF is the binding site for <scene name='77/778327/Ibalpha/1'>glycoprotein Ib alpha</scene> and for collagen. The A2 domain is responsible for binding the cleavage site to ADAMTS-13. ADAMTS-13 is a metalloprotease that cleaves the VWF. | ||
== Disease == | == Disease == | ||
- | As VWF plays a role in coagulation, defects in the VWF leads to a bleeding disorder called von Willebrand Disease that affects 0.01%-1% of the population. | ||
== Structural highlights == | == Structural highlights == |
Revision as of 14:27, 30 April 2018
This Sandbox is Reserved from Jan 22 through May 22, 2018 for use in the course Biochemistry II taught by Jason Telford at the Maryville University, St. Louis, Missouri, USA. This reservation includes Sandbox Reserved 1446 through Sandbox Reserved 1455. |
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von Willebrand Factor
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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
1. Desch, K. C. (2018). Regulation of plasma von Willebrand factor. F1000Research, 7, 96. http://doi.org/10.12688/f1000research.13056.1