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Sandbox Reserved 165

This Sandbox is Reserved from March 9, 2011, through May 30, 2011 for use by the course Biochemistry at Reinhardt University, Waleska, USA, taught by Irma Santoro. This reservation includes Sandbox Reserved 162 through Sandbox Reserved 168.
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<Structure load='2hh0' size='500' frame='true' align='right' caption='2HH0 Protein' scene='Insert optional scene name here' ->

Prion Protein (2HH0)Prion Protein (2HH0)

2HH0 is a prion protein that manifests in bovine(cattle) and can lead to degenerative central nervous system tissues. The word “prion” is derived from “protein + infection.” Prions were discovered in 1997 by Stanley B. Prusiner of the University of California. [1] They are infected proteins and may lay dormant for many years before they activate and cause damage to the brain and spinal cord. [2]


StructureStructure

2HH0 is a crystal structured beta-protein. It has seven strands and a “Greek key” sandwich structure. 2HH0 is a carrier protein. [2]

Role in DiseaseRole in Disease

Prion diseases are named differently, depending on which species they affect. In sheep, the disease is called scrapie; in humans, it is called Creutzfeldt-Jakob(CJD) and named for two German researchers; in deer and elk, it is chronic wasting disease; and in cattle, it is mad cow disease. [3] For reasons that are not clear, prions unfold and create holes in the central nervous system. Cases of bovine spongioform encephalopathy (BSE), or “mad cow disease,” were identified in 1986 in British cattle. Nine years later, almost half the British herds had been affected and led to the demise of more than 150,000 cattle. [4] This caused the United States and many other countries to refuse blood tranfusions from anyone who had spent more than three months in the United Kingdom from 1986 through 1996. There are three ways in which a prion disease may be contracted: infection caused by the consumption of infected tissues or contaminated equipment used in medical procedures, hereditary transmission, or spontaneous formation of the disease. [5] Over 200 Americans died in 2000 of CJD. [6]


ReferencesReferences

  1. ↑ Prusiner, S. Autobiography. Retrieved March 25, 2011, from NobelPrize.org Web site:http//nobelprize.org/nobel_prizes/medicine/laureates/1997/prusiner-autobio.html.
  2. ↑ 2.0 2.1 Luginbuhl, B., Kanyo, Z., Jones, R.M., Fletterick, R.J., Prusiner, S.B., Cohen, F.E., Williamson, R.A., Burton, D.R., & Pluckthun, A. Directed evolution of an anti-prion protein scFv fragment to an affinity of 1 pM and its structural interpretation. 2006. J.Mol.Biol. 2006 363:75-97. Cite error: Invalid <ref> tag; name "Luginbuhl, B." defined multiple times with different content
  3. ↑ Telling, B. Prions and Prion Diseases:Current Perspectives. 2004. Horizon Bioscience. 307.
  4. ↑ Yam, P. (2009, September). Mad Cow Disease. Scientific American, 301(3), 89.
  5. ↑ Appleby, B. Psychotropic Medications and the Treatment of Human Prion Diseases. CNS & Neurological Disorders-Drug Targets. 2009. 8(5):353-362.
  6. ↑ Holman, R., Belay, E.,Christensen, K., Maddox, R., Mininio, A., Folkema, A., Haberling, D., Hammett, T., Kochanek, K., &Sejvar, J. Human Prion Diseases in the United States. PLoS ONE 5(1): e8521. doi:10.1371/journal.pone.0008521.

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