3nvh

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[[Image:3nvh.png|left|200px]]
 
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{{STRUCTURE_3nvh| PDB=3nvh | SCENE= }}
{{STRUCTURE_3nvh| PDB=3nvh | SCENE= }}
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===MIHFGND segment 137-143 from mouse prion===
===MIHFGND segment 137-143 from mouse prion===
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{{ABSTRACT_PUBMED_21323366}}
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{{ABSTRACT_PUBMED_21323366}}
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==Disease==
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[[http://www.uniprot.org/uniprot/PRIO_MOUSE PRIO_MOUSE]] 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.
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==Function==
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[[http://www.uniprot.org/uniprot/PRIO_MOUSE PRIO_MOUSE]] 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) (By similarity). 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.<ref>PMID:12732622</ref><ref>PMID:16492732</ref><ref>PMID:19242475</ref><ref>PMID:19568430</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:021323366</ref><references group="xtra"/>
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<ref group="xtra">PMID:021323366</ref><references group="xtra"/><references/>
[[Category: Apostol, M I.]]
[[Category: Apostol, M I.]]
[[Category: Eisenberg, D.]]
[[Category: Eisenberg, D.]]

Revision as of 22:48, 24 March 2013

Template:STRUCTURE 3nvh

Contents

MIHFGND segment 137-143 from mouse prion

Template:ABSTRACT PUBMED 21323366

Disease

[PRIO_MOUSE] 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

[PRIO_MOUSE] 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) (By similarity). 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.[1][2][3][4]

About this Structure

3nvh is a 1 chain structure. Full crystallographic information is available from OCA.

See Also

Reference

  • Apostol MI, Wiltzius JJ, Sawaya MR, Cascio D, Eisenberg D. Atomic structures suggest determinants of transmission barriers in mammalian prion disease. Biochemistry. 2011 Feb 16. PMID:21323366 doi:10.1021/bi101803k
  1. ↑ Mani K, Cheng F, Havsmark B, Jonsson M, Belting M, Fransson LA. Prion, amyloid beta-derived Cu(II) ions, or free Zn(II) ions support S-nitroso-dependent autocleavage of glypican-1 heparan sulfate. J Biol Chem. 2003 Oct 3;278(40):38956-65. Epub 2003 May 5. PMID:12732622 doi:10.1074/jbc.M300394200
  2. ↑ Steele AD, Emsley JG, Ozdinler PH, Lindquist S, Macklis JD. Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis. Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3416-21. Epub 2006 Feb 21. PMID:16492732 doi:10.1073/pnas.0511290103
  3. ↑ Lauren J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature. 2009 Feb 26;457(7233):1128-32. doi: 10.1038/nature07761. PMID:19242475 doi:10.1038/nature07761
  4. ↑ Singh A, Kong Q, Luo X, Petersen RB, Meyerson H, Singh N. Prion protein (PrP) knock-out mice show altered iron metabolism: a functional role for PrP in iron uptake and transport. PLoS One. 2009 Jul 1;4(7):e6115. doi: 10.1371/journal.pone.0006115. PMID:19568430 doi:10.1371/journal.pone.0006115

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