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Prion protein (p27-30) (Creutzfeldt-Jakob disease, Gerstmann-Strausler-Scheinker syndrome, fatal familial insomnia)

PDB rendering based on 1ag2.
Available structures
1ag2, 1dwy, 1dwz, 1dx0, 1dx1, 1e1g, 1e1j, 1e1p, 1e1s, 1e1u, 1e1w, 1fkc, 1fo7, 1h0l, 1hjm, 1hjn, 1i4m, 1oei, 1qlx, 1qlz, 1qm0, 1qm1, 1qm2, 1qm3, 1tpx, 1tqb, 1tqc, 1uw3, 1xyu, 1xyx, 1y15, 1y2s
Symbols PRNP; GSS; ASCR; CD230; CJD; MGC26679; PRIP; PrP; PrP27-30; PrP33-35C; PrPc
External IDs OMIM176640 MGI97769 HomoloGene7904 GeneCards: PRNP Gene
RNA expression pattern
PBB GE PRNP 201300 s at tn.png
PBB GE PRNP 215707 s at tn.png
More reference expression data
Species Human Mouse
Entrez 5621 19122
Ensembl ENSG00000171867 n/a
UniProt P04156 n/a
RefSeq (mRNA) NM_000311 NM_011170
RefSeq (protein) NP_000302 NP_035300
Location (UCSC) Chr 20:
4.61 - 4.63 Mb
PubMed search [1] [2]

PRNP (PRioN Protein (Creutzfeld-Jakob disease, Gerstmann-Sträussler-Scheinker syndrome, fatal familial insomnia)) is a gene[1][2][3][4] that codes for a protein called the prion protein (PrP), which is expressed in the brain and several other tissues.[5][6]

The human PRNP gene is located on the short (p) arm of chromosome 20 between the end (terminus) of the arm and position 12, from base pair 4,615,068 to base pair 4,630,233.

PRNP has also recently been designated CD230 (cluster of differentiation 230).



Although the precise function of PrP is not yet known, it is possibly involved in the transport of ionic copper to cells from the surrounding environment. Researchers have also proposed roles for PrP in cell signaling or in the formation of gaps between nerve cells (synapses) where cell-to-cell communication occurs.

Different forms of PrP have been identified in the nervous system. The usual cellular form is called PrPC. Another form, PrPSc, has a different 3-dimensional structure and has been associated with inherited, sporadic, and infectious disorders of the brain and nervous system. In a process that is not fully understood, PrPC is transformed into the infectious isomer PrPSc. This abnormal protein can further promote the transformation of PrPC into nascent PrPSc, leading to transmissible spongiform encephalopathy.

Disease linkage

More than 20 mutations in the PRNP gene have been identified in people with inherited prion diseases, which include the following:[7][8]

Some PRNP mutations lead to a change in single amino acids (the building blocks of proteins) in the prion protein. Others insert additional amino acids into the protein or cause an abnormally short protein to be made. These mutations cause the cell to make prion proteins with an abnormal structure. The abnormal protein, PrPSc, accumulates in the brain and destroys nerve cells, which leads to the mental and behavioral features of prion diseases.

Several other changes in the PRNP gene (called polymorphisms) do not cause prion diseases, but may affect a person's risk of developing these diseases or alter the course of the disorders. An allele which codes for a PRNP variant — G127V provides resistance to Kuru.[11][12]


PRNP has been shown to interact with Hop.[13]


  1. ^ Kretzschmar HA, Stowring LE, Westaway D, Stubblebine WH, Prusiner SB, Dearmond SJ (August 1986). "Molecular cloning of a human prion protein cDNA". DNA 5 (4): 315–24. PMID 3755672.  
  2. ^ Sparkes RS, Simon M, Cohn VH, et al. (October 1986). "Assignment of the human and mouse prion protein genes to homologous chromosomes". Proc. Natl. Acad. Sci. U.S.A. 83 (19): 7358–62. doi:10.1073/pnas.83.19.7358. PMID 3094007. PMC 386716.  
  3. ^ Liao YC, Lebo RV, Clawson GA, Smuckler EA (July 1986). "Human prion protein cDNA: molecular cloning, chromosomal mapping, and biological implications". Science (journal) 233 (4761): 364–7. PMID 3014653.  
  4. ^ Robakis NK, Devine-Gage EA, Jenkins EC, et al. (October 1986). "Localization of a human gene homologous to the PrP gene on the p arm of chromosome 20 and detection of PrP-related antigens in normal human brain". Biochem. Biophys. Res. Commun. 140 (2): 758–65. doi:10.1016/0006-291X(86)90796-5. PMID 2877664.  
  5. ^ Prusiner SB (2001). "Shattuck lecture--neurodegenerative diseases and prions". N Engl J Med 344 (20): 1516–26. doi:10.1056/NEJM200105173442006. PMID 11357156.  
  6. ^ Weissmann C (2004). "The state of the prion". Nat Rev Microbiol 2 (11): 861–71. doi:10.1038/nrmicro1025. PMID 15494743.  
  7. ^ Castilla J, Hetz C, Soto C (2004). "Molecular mechanisms of neurotoxicity of pathological prion protein". Curr Mol Med 4 (4): 397–403. doi:10.2174/1566524043360654. PMID 15354870.  
  8. ^ Kovacs GG, Trabattoni G, Hainfellner JA, Ironside JW, Knight RS, Budka H (2002). "Mutations of the prion protein gene phenotypic spectrum". J Neurol 249 (11): 1567–82. doi:10.1007/s00415-002-0896-9. PMID 12420099.  
  9. ^ Collins S, McLean CA, Masters CL (2001). "Gerstmann-Straussler-Scheinker syndrome,fatal familial insomnia, and kuru: a review of these less common human transmissible spongiform encephalopathies". J Clin Neurosci 8 (5): 387–97. doi:10.1054/jocn.2001.0919. PMID 11535002.  
  10. ^ Montagna P, Gambetti P, Cortelli P, Lugaresi E (2003). "Familial and sporadic fatal insomnia". Lancet Neurol 2 (3): 167–76. doi:10.1016/S1474-4422(03)00323-5. PMID 12849238.  
  11. ^ Medical Research Council (UK) ((November 21, 2009)). "Brain Disease 'Resistance Gene' Evolves in Papua New Guinea Community; Could Offer Insights Into CJD". Science Daily (online) (Science News). Retrieved 2009-11-22.  
  12. ^ Mead, S.; Whitfield, J.; Poulter, M.; Shah, P.; Uphill, J.; Campbell, T.; Al-Dujaily, H.; Hummerich, H. et al. (2009). "A Novel Protective Prion Protein Variant that Colocalizes with Kuru Exposure.". The New England journal of medicine 361 (21): 2056–2065. doi:10.1056/NEJMoa0809716. PMID 19923577.   edit
  13. ^ Zanata, Silvio M; Lopes Marilene H, Mercadante Adriana F, Hajj Glaucia N M, Chiarini Luciana B, Nomizo Regina, Freitas Adriana R O, Cabral Ana L B, Lee Kil S, Juliano Maria A, de Oliveira Elizabeth, Jachieri Saul G, Burlingame Alma, Huang Lan, Linden Rafael, Brentani Ricardo R, Martins Vilma R (Jul. 2002). "Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection". EMBO J. (England) 21 (13): 3307–16. doi:10.1093/emboj/cdf325. ISSN 0261-4189. PMID 12093732.  

External links

External links



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