1e1u: Difference between revisions

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[[Image:1e1u.jpg|left|200px]]
[[Image:1e1u.jpg|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e1u OCA], [http://www.ebi.ac.uk/pdbsum/1e1u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e1u RCSB]</span>
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'''HUMAN PRION PROTEIN VARIANT R220K'''
'''HUMAN PRION PROTEIN VARIANT R220K'''
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[[Category: Wuthrich, K.]]
[[Category: Wuthrich, K.]]
[[Category: Zahn, R.]]
[[Category: Zahn, R.]]
[[Category: prion protein]]
[[Category: Prion protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:33:17 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:53:17 2008''

Revision as of 14:33, 2 May 2008

File:1e1u.jpg

Template:STRUCTURE 1e1u

HUMAN PRION PROTEIN VARIANT R220K


OverviewOverview

The NMR structures of three single-amino acid variants of the C-terminal domain of the human prion protein, hPrP(121-230), are presented. In hPrP(M166V) and hPrP(R220K) the substitution is with the corresponding residue in murine PrP, and in hPrP(S170N) it is with the corresponding Syrian hamster residue. All three substitutions are in the surface region of the structure of the cellular form of PrP (PrP(C)) that is formed by the C-terminal part of helix 3, with residues 218-230, and a loop of residues 166-172. This molecular region shows high species variability and has been implicated in specific interactions with a so far not further characterized "protein X," and it is related to the species barrier for transmission of prion diseases. As expected, the three variant hPrP(121-230) structures have the same global architecture as the previously determined wild-type bovine, human, murine, and Syrian hamster prion proteins, but with the present study two localized "conformational markers" could be related with single amino acid exchanges. These are the length and quality of definition of helix 3, and the NMR-observability of the residues in the loop 166-172. Poor definition of the C-terminal part of helix 3 is characteristic for murine PrP and has now been observed also for hPrP(R220K), and NMR observation of the complete loop 166-172 has so far been unique for Syrian hamster PrP and is now also documented for hPrP(S170N).

About this StructureAbout this Structure

1E1U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

NMR structures of three single-residue variants of the human prion protein., Calzolai L, Lysek DA, Guntert P, von Schroetter C, Riek R, Zahn R, Wuthrich K, Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8340-5. PMID:10900000 Page seeded by OCA on Fri May 2 14:33:17 2008

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