Sandbox Reserved 165: Difference between revisions
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== 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 an spinal cord. <ref name="Insert name">McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100</ref> | |||
== Structure == | == Structure == | ||
2HH0 is a crystal structured beta-protein. It has seven strands and a “Greek key” sandwich structure. PDP Protein Data Bank | |||
== Role in Disease == | == Role in Disease == |
Revision as of 12:10, 30 March 2011
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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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 an spinal cord. [1]
StructureStructure
2HH0 is a crystal structured beta-protein. It has seven strands and a “Greek key” sandwich structure. PDP Protein Data Bank
Role in DiseaseRole in Disease
more info
ReferencesReferences
- ↑ McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100