1skh
From Proteopedia
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{{STRUCTURE_1skh| PDB=1skh | SCENE= }} | {{STRUCTURE_1skh| PDB=1skh | SCENE= }} | ||
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===N-terminal (1-30) of bovine Prion protein=== | ===N-terminal (1-30) of bovine Prion protein=== | ||
| + | {{ABSTRACT_PUBMED_15554701}} | ||
| - | + | ==Disease== | |
| + | [[http://www.uniprot.org/uniprot/PRIO_BOVIN PRIO_BOVIN]] Note=Variations in PRNP are responsible of transmissible bovine spongiform encephalopathies (BSE), a class of neurodegenerative diseases that affect various mammals. These diseases are caused by abnormally folded prion proteins. BSE can be subdivided into at least three groups: classical, H-type and L-type, with the latter 2 collectively referred to as atypical BSE. Susceptibility or resistance to a BSE disease can be influenced by at least 3 factors related to the host prion protein: protein expression levels, number of octapeptide repeats, and specific polymorphisms. In cattle, as in humans, BSEs can occur as infectious, spontaneous and genetic diseases. | ||
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| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/PRIO_BOVIN PRIO_BOVIN]] 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). | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:015554701</ref><references group="xtra"/> | + | <ref group="xtra">PMID:015554701</ref><references group="xtra"/><references/> |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Prions]] | [[Category: Prions]] | ||
Revision as of 23:31, 24 March 2013
Contents |
N-terminal (1-30) of bovine Prion protein
Template:ABSTRACT PUBMED 15554701
Disease
[PRIO_BOVIN] Note=Variations in PRNP are responsible of transmissible bovine spongiform encephalopathies (BSE), a class of neurodegenerative diseases that affect various mammals. These diseases are caused by abnormally folded prion proteins. BSE can be subdivided into at least three groups: classical, H-type and L-type, with the latter 2 collectively referred to as atypical BSE. Susceptibility or resistance to a BSE disease can be influenced by at least 3 factors related to the host prion protein: protein expression levels, number of octapeptide repeats, and specific polymorphisms. In cattle, as in humans, BSEs can occur as infectious, spontaneous and genetic diseases.
Function
[PRIO_BOVIN] 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).
About this Structure
1skh is a 1 chain structure with sequence from Bos taurus. The May 2008 RCSB PDB Molecule of the Month feature on Prions by David S. Goodsell is 10.2210/rcsb_pdb/mom_2008_5. Full experimental information is available from OCA.
See Also
Reference
- Biverstahl H, Andersson A, Graslund A, Maler L. NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein. Biochemistry. 2004 Nov 30;43(47):14940-7. PMID:15554701 doi:10.1021/bi0485070
