1ag2

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[[Image:1ag2.gif|left|200px]]
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{{Structure
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|GENE= T7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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{{STRUCTURE_1ag2| PDB=1ag2 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ag2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ag2 OCA], [http://www.ebi.ac.uk/pdbsum/1ag2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ag2 RCSB]</span>
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'''PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, 2 MINIMIZED AVERAGE STRUCTURE'''
'''PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, 2 MINIMIZED AVERAGE STRUCTURE'''
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[[Category: Wider, G.]]
[[Category: Wider, G.]]
[[Category: Wuthrich, K.]]
[[Category: Wuthrich, K.]]
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[[Category: brain]]
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[[Category: Brain]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: gpi-anchor]]
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[[Category: Gpi-anchor]]
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[[Category: prion protein]]
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[[Category: Prion protein]]
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Revision as of 07:13, 2 May 2008

Template:STRUCTURE 1ag2

PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, 2 MINIMIZED AVERAGE STRUCTURE


Overview

The 'protein only' hypothesis states that a modified form of normal prion protein triggers infectious neurodegenerative diseases, such as bovine spongiform encephalopathy (BSE), or Creutzfeldt-Jakob disease (CJD) in humans. Prion proteins are thought to exist in two different conformations: the 'benign' PrPcform, and the infectious 'scrapie form', PrPsc. Knowledge of the three-dimensional structure of PrPc is essential for understanding the transition to PrPsc. The nuclear magnetic resonance (NMR) structure of the autonomously folding PrP domain comprising residues 121-231 (ref. 6) contains a two-stranded antiparallel beta-sheet and three alpha-helices. This domain contains most of the point-mutation sites that have been linked, in human PrP, to the occurrence of familial prion diseases. The NMR structure shows that these mutations occur within, or directly adjacent to, regular secondary structures. The presence of a beta-sheet in PrP(121-231) is in contrast with model predictions of an all-helical structure of PrPc (ref. 8), and may be important for the initiation of the transition from PrPc to PrPsc.

About this Structure

1AG2 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

NMR structure of the mouse prion protein domain PrP(121-321)., Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wuthrich K, Nature. 1996 Jul 11;382(6587):180-2. PMID:8700211 Page seeded by OCA on Fri May 2 10:13:16 2008

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