1ag2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE= T7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
|GENE= T7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|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>
}}
}}
Line 33: Line 36:
[[Category: prion protein]]
[[Category: prion protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:57:00 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:39:26 2008''

Revision as of 15:39, 30 March 2008


PDB ID 1ag2

Drag the structure with the mouse to rotate
Gene: T7 (Mus musculus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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 Sun Mar 30 18:39:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools