1e1s: Difference between revisions
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'''HUMAN PRION PROTEIN VARIANT S170N''' | {{Structure | ||
|PDB= 1e1s |SIZE=350|CAPTION= <scene name='initialview01'>1e1s</scene> | |||
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'''HUMAN PRION PROTEIN VARIANT S170N''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E1S is a [ | 1E1S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E1S OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10900000 10900000] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: prion protein]] | [[Category: prion protein]] | ||
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Revision as of 11:48, 20 March 2008
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HUMAN PRION PROTEIN VARIANT S170N
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).
DiseaseDisease
Known diseases associated with this structure: Creutzfeldt-Jakob disease OMIM:[176640], Gerstmann-Straussler disease OMIM:[176640], Huntington disease-like 1 OMIM:[176640], Insomnia, fatal familial OMIM:[176640], Prion disease with protracted course OMIM:[176640], Retinitis pigmentosa-11 OMIM:[606419]
About this StructureAbout this Structure
1E1S 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
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