1b10: Difference between revisions
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{{STRUCTURE_1b10| PDB=1b10 | SCENE= }} | {{STRUCTURE_1b10| PDB=1b10 | SCENE= }} | ||
===SOLUTION NMR STRUCTURE OF RECOMBINANT SYRIAN HAMSTER PRION PROTEIN RPRP(90-231) , 25 STRUCTURES=== | |||
{{ABSTRACT_PUBMED_9294167}} | |||
=== | ==Disease== | ||
[[http://www.uniprot.org/uniprot/PRIO_MESAU PRIO_MESAU]] Note=Found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc. | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/PRIO_MESAU PRIO_MESAU]] May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).<ref>PMID:19059915</ref> | |||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:009294167</ref><references group="xtra"/> | <ref group="xtra">PMID:009294167</ref><references group="xtra"/><references/> | ||
[[Category: Mesocricetus auratus]] | [[Category: Mesocricetus auratus]] | ||
[[Category: Farr-Jones, S.]] | [[Category: Farr-Jones, S.]] | ||
Revision as of 05:35, 25 March 2013
SOLUTION NMR STRUCTURE OF RECOMBINANT SYRIAN HAMSTER PRION PROTEIN RPRP(90-231) , 25 STRUCTURESSOLUTION NMR STRUCTURE OF RECOMBINANT SYRIAN HAMSTER PRION PROTEIN RPRP(90-231) , 25 STRUCTURES
Template:ABSTRACT PUBMED 9294167
DiseaseDisease
[PRIO_MESAU] Note=Found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc.
FunctionFunction
[PRIO_MESAU] May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).[1]
About this StructureAbout this Structure
1b10 is a 1 chain structure with sequence from Mesocricetus auratus. This structure supersedes the now removed PDB entry 2prp. Full experimental information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ James TL, Liu H, Ulyanov NB, Farr-Jones S, Zhang H, Donne DG, Kaneko K, Groth D, Mehlhorn I, Prusiner SB, Cohen FE. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc Natl Acad Sci U S A. 1997 Sep 16;94(19):10086-91. PMID:9294167
- ↑ Juanes ME, Elvira G, Garcia-Grande A, Calero M, Gasset M. Biosynthesis of prion protein nucleocytoplasmic isoforms by alternative initiation of translation. J Biol Chem. 2009 Jan 30;284(5):2787-94. doi: 10.1074/jbc.M804051200. Epub 2008, Dec 5. PMID:19059915 doi:10.1074/jbc.M804051200